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(-) Description

Title :  THE ACTIVE SITE OF A CARBOHYDRATE ESTERASE DISPLAYS DIVERGENT CATALYTIC AND NON-CATALYTIC BINDING FUNCTIONS
 
Authors :  C. Montanier, V. A. Money, V. Pires, J. E. Flint, P. A. Benedita, A. Goyal J. A. Prates, A. Izumi, H. Stalbrand, C. Morland, A. Cartmell, K. Kolen E. Topakas, E. Dobson, D. N. Bolam, G. J. Davies, C. M. Fontes, H. J. Gilb
Date :  29 Jan 09  (Deposition) - 24 Mar 09  (Release) - 13 Jul 11  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.00
Chains :  Asym./Biol. Unit :  A,B
Keywords :  Carbohydrate Esterase Family 2, Hydrolase, Acetyl Xylan Esterase (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  C. Montanier, V. A. Money, V. Pires, J. E. Flint, P. A. Benedita, A. Goyal, J. A. Prates, A. Izumi, H. Stalbrand, C. Morland, A. Cartmell K. Kolenova, E. Topakas, E. J. Dodson, D. N. Bolam, G. J. Davies, C. M. Fontes, H. J. Gilbert
The Active Site Of A Carbohydrate Esterase Displays Divergent Catalytic And Noncatalytic Binding Functions.
Plos Biol. V. 7 E71 2009
PubMed-ID: 19338387  |  Reference-DOI: 10.1371/JOURNAL.PBIO.1000071

(-) Compounds

Molecule 1 - PUTATIVE ACETYL XYLAN ESTERASE
    Chains: A, B
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Plasmid: PET22B
    Expression System Strain: BL21(DE3)
    Expression System Taxid: 469008
    Organism Scientific: CELLVIBRIO JAPONICUS
    Organism Taxid: 155077
    Synonym: AXE2A, CJCE2B

 Structural Features

(-) Chains, Units

  12
Asymmetric/Biological Unit : AB

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 7)

Asymmetric/Biological Unit (1, 7)
No.NameCountTypeFull Name
1GOL7Ligand/IonGLYCEROL

(-) Sites  (7, 7)

Asymmetric Unit (7, 7)
No.NameEvidenceResiduesDescription
1AC1SOFTWARESER A:151 , GLY A:199 , HIS A:336 , HOH A:2097 , HOH A:2185BINDING SITE FOR RESIDUE GOL A1362
2AC2SOFTWAREGLY A:199 , PHE A:200 , THR A:209 , SER A:210 , HOH A:2186 , HOH A:2187BINDING SITE FOR RESIDUE GOL A1363
3AC3SOFTWAREGLU A:116 , GLN A:118 , TYR A:156 , THR A:174 , HOH A:2028BINDING SITE FOR RESIDUE GOL A1364
4AC4SOFTWARESER B:151 , TYR B:156 , GLY B:199 , HIS B:336 , HOH B:2075 , HOH B:2229BINDING SITE FOR RESIDUE GOL B1362
5AC5SOFTWAREGLY B:199 , PHE B:200 , THR B:209 , SER B:210 , HOH B:2230BINDING SITE FOR RESIDUE GOL B1363
6AC6SOFTWAREGLU B:116 , GLN B:118 , PHE B:171 , HOH B:2053 , HOH B:2231BINDING SITE FOR RESIDUE GOL B1364
7AC7SOFTWAREASP A:295 , HOH A:2159 , ASP B:295 , GLN B:296 , GLY B:327 , LEU B:328 , TYR B:330BINDING SITE FOR RESIDUE GOL B1365

(-) SS Bonds  (2, 2)

Asymmetric/Biological Unit
No.Residues
1A:165 -A:333
2B:165 -B:333

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 2W9X)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2W9X)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 2W9X)

(-) Exons   (0, 0)

(no "Exon" information available for 2W9X)

(-) Sequences/Alignments

Asymmetric/Biological Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it) 
Chain A from PDB  Type:PROTEIN  Length:312
 aligned with CE2B_CELJU | B3PDE5 from UniProtKB/Swiss-Prot  Length:360

    Alignment length:335
                                                                                                                                                                                                                                                                                                                                                                       360 
                                    36        46        56        66        76        86        96       106       116       126       136       146       156       166       176       186       196       206       216       226       236       246       256       266       276       286       296       306       316       326       336       346       356   | 
           CE2B_CELJU    27 PLPLHIGGRVLVESPANQPVSYTYSWPAVYFETAFKGQSLTLKFDDDQNIFRLIVDDKAPVVINKPGKVDYPVESLAPGKHRVRLEKLTETQSTSGRFLGFYTDPSAKPLALPKRKRQIEFIGDSFTVGYGNTSPSRECTDEELFKTTNSQMAFGPLTAKAFDADYQINASSGFGIVRNYNGTSPDKSLLSLYPYTLNNPDQLYHNKHWKPQVIVIGLGTNDFSTALNDNERWKTREALHADYVANYVKFVKQLHSNNARAQFILMNSDQSNGEIAEQVGKVVAQLKGGGLHQVEQIVFKGLDYSGCHWHPSANDDQLLANLLITHLQQKKGIW-   -
               SCOP domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ....eee...eee..--...eeee.....eeee..-.....eeeee...eeeee.--...eeee..eeeee.---------.eeeee........eee...---------.......eeeeeehhhhhh..........hhhhhhhhhhhhhhhhhhhhhhh..eeeeee........hhhhh....hhhhhh...................eeeee.hhhhhh..........hhhhhhhhhhhhhhhhhhhhhhhh...eeeeeee.hhhhhhhhhhhhhhhhhhhh....eeeeee.......hhh..hhhhhhhhhhhhhhhhhh...... Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2w9x A  27 PLPLHIGGRVLVESP--QPVSYTYSWPAVYFETAF-GQSLTLKFDDDQNIFRLIV--KAPVVINKPGKVDYP---------RVRLEKLTETQSTSGRFLGF---------ALPKRKRQIEFIGDSFTVGYGNTSPSRECTDEELFKTTNSQMAFGPLTAKAFDADYQINASSGFGIVRNYNGTSPDKSLLSLYPYTLNNPDQLYHNKHWKPQVIVIGLGTNDFSTALNDNERWKTREALHADYVANYVKFVKQLHSNNARAQFILMNSDQSNGEIAEQVGKVVAQLKGGGLHQVEQIVFKGLDYSGCHWHPSANDDQLLANLLITHLQQKKGIWL 361
                                    36    |  |46        56    | | 66        76    |  |86        96 |       - |     116       126|        -|      146       156       166       176       186       196       206       216       226       236       246       256       266       276       286       296       306       316       326       336       346       356     
                                         41 44               61 |                81 84            98       108                127       137                                                                                                                                                                                                                                
                                                               63                                                                                                                                                                                                                                                                                                          


Chain B from PDB  Type:PROTEIN  Length:329
 aligned with CE2B_CELJU | B3PDE5 from UniProtKB/Swiss-Prot  Length:360

    Alignment length:336
                                                                                                                                                                                                                                                                                                                                                                        360 
                                    35        45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205       215       225       235       245       255       265       275       285       295       305       315       325       335       345       355    | 
           CE2B_CELJU    26 KPLPLHIGGRVLVESPANQPVSYTYSWPAVYFETAFKGQSLTLKFDDDQNIFRLIVDDKAPVVINKPGKVDYPVESLAPGKHRVRLEKLTETQSTSGRFLGFYTDPSAKPLALPKRKRQIEFIGDSFTVGYGNTSPSRECTDEELFKTTNSQMAFGPLTAKAFDADYQINASSGFGIVRNYNGTSPDKSLLSLYPYTLNNPDQLYHNKHWKPQVIVIGLGTNDFSTALNDNERWKTREALHADYVANYVKFVKQLHSNNARAQFILMNSDQSNGEIAEQVGKVVAQLKGGGLHQVEQIVFKGLDYSGCHWHPSANDDQLLANLLITHLQQKKGIW-   -
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author .....eee...eee.......eeee.....eeeeeee....eeeeee...eeeeee.....eeee..eeeeee.-------.eeeeee........eeeeeee.....ee........eeeeeehhhhhh..........hhhhhhhhhhhhhhhhhhhhhhh..eeeeee........hhhhh....hhhhhh...................eeeee.hhhhhh..........hhhhhhhhhhhhhhhhhhhhhhhh...eeeeeee.hhhhhhhhhhhhhhhhhhhh....eeeeee............hhhhhhhhhhhhhhhhhh...... Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                 2w9x B  26 KPLPLHIGGRVLVESPANQPVSYTYSWPAVYFETAFKGQSLTLKFDDDQNIFRLIVDDKAPVVINKPGKVDYPV-------HRVRLEKLTETQSTSGRFLGFYTDPSAKPLALPKRKRQIEFIGDSFTVGYGNTSPSRECTDEELFKTTNSQMAFGPLTAKAFDADYQINASSGFGIVRNYNGTSPDKSLLSLYPYTLNNPDQLYHNKHWKPQVIVIGLGTNDFSTALNDNERWKTREALHADYVANYVKFVKQLHSNNARAQFILMNSDQSNGEIAEQVGKVVAQLKGGGLHQVEQIVFKGLDYSGCHWHPSANDDQLLANLLITHLQQKKGIWL 361
                                    35        45        55        65        75        85        95   |     - |     115       125       135       145       155       165       175       185       195       205       215       225       235       245       255       265       275       285       295       305       315       325       335       345       355      
                                                                                                    99     107
   Legend:   → Mismatch (orange background)
  - → Gap (green background, '-', border residues have a numbering label)
    → Modified Residue (blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 2W9X)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2W9X)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 2W9X)

(-) Gene Ontology  (10, 10)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A,B   (CE2B_CELJU | B3PDE5)
molecular function
    GO:0046555    acetylxylan esterase activity    Catalysis of the deacetylation of xylans and xylo-oligosaccharides.
    GO:0016787    hydrolase activity    Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
    GO:0016788    hydrolase activity, acting on ester bonds    Catalysis of the hydrolysis of any ester bond.
    GO:0016798    hydrolase activity, acting on glycosyl bonds    Catalysis of the hydrolysis of any glycosyl bond.
biological process
    GO:0005975    carbohydrate metabolic process    The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
    GO:2000884    glucomannan catabolic process    The chemical reactions and pathways resulting in the breakdown of a glucomannan.
    GO:0008152    metabolic process    The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
    GO:0000272    polysaccharide catabolic process    The chemical reactions and pathways resulting in the breakdown of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
    GO:0045493    xylan catabolic process    The chemical reactions and pathways resulting in the breakdown of xylan, a polymer containing a beta-1,4-linked D-xylose backbone.
cellular component
    GO:0005576    extracellular region    The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

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 Related Entries

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(-) Related Entries Specified in the PDB File

2waa STRUCTURE OF A FAMILY TWO CARBOHYDRATE ESTERASE FROM CELLVIBRIO JAPONICUS
2wab STRUCTURE OF AN ACTIVE SITE MUTANT OF A FAMILY TWO CARBOHYDRATE ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH CELLUOHEXASE
2wao STRUCTURE OF A FAMILY TWO CARBOHYDRATE ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH CELLOHEXAOSE