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(-) Description

Title :  C-TERMINAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE 11A
 
Authors :  P. J. Simpson, X. Hefang, D. N. Bolam, P. White, S. M. Hancock, H. J. Gilbert, M. P. Williamson
Date :  22 Nov 00  (Deposition) - 10 May 01  (Release) - 24 Feb 09  (Revision)
Method :  SOLUTION NMR
Resolution :  NOT APPLICABLE
Chains :  NMR Structure  :  C  (5x)
Keywords :  Hydrolase(Xylan Degradation), Hydrolase, Xylan Binding Domain, Xylanase, Beta-Sheet (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  D. N. Bolam, H. Xie, P. White, P. J. Simpson, S. M. Hancock, M. P. Williamson, H. J. Gilbert
Evidence For Synergy Between Family 2B Carbohydrate Binding Modules In Cellulomonas Fimi Xylanase 11A
Biochemistry V. 40 2468 2001
PubMed-ID: 11327868  |  Reference-DOI: 10.1021/BI002564L

(-) Compounds

Molecule 1 - ENDO-1,4-BETA-XYLANASE D
    ChainsC
    EC Number3.2.1.8
    EngineeredYES
    Expression SystemESCHERICHIA COLI
    Expression System StrainBL21(DE3)
    Expression System Taxid469008
    FragmentXYLAN BINDING DOMAIN 2
    Organism ScientificCELLULOMONAS FIMI
    Organism Taxid1708
    StrainJM83
    SynonymXYLANASE D, CBM2B-2, XBD2

 Structural Features

(-) Chains, Units

  
NMR Structure (5x)

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (0, 0)

(no "Ligand,Modified Residues,Ions" information available for 1HEJ)

(-) Sites  (0, 0)

(no "Site" information available for 1HEJ)

(-) SS Bonds  (1, 1)

NMR Structure
No.Residues
1C:560 -C:641

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 1HEJ)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 1HEJ)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 1HEJ)

(-) Exons   (0, 0)

(no "Exon" information available for 1HEJ)

(-) Sequences/Alignments

NMR Structure
   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
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Chain C from PDB  Type:PROTEIN  Length:88
 aligned with XYND_CELFI | P54865 from UniProtKB/Swiss-Prot  Length:644

    Alignment length:88
                                   566       576       586       596       606       616       626       636        
           XYND_CELFI   557 TGSCSVSAVRGEEWADRFNVTYSVSGSSSWVVTLGLNGGQSVQSSWNAALTGSSGTVTARPNGSGNSFGVTFYKNGSSATPGATCATG 644
               SCOP domains d1hejc_ C: Endo-1,4-beta xylanase D, xylan binding domain, XBD                           SCOP domains
               CATH domains 1hejC00 C:557-644  [code=2.60.40.290, no name defined]                                   CATH domains
               Pfam domains ---------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .....eeeeeee....eeeeeeeee.....eeeeee.....eeeee..eeee....eeee......eeeeeee........eeeee.. Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ---------------------------------------------------------------------------------------- PROSITE
                 Transcript ---------------------------------------------------------------------------------------- Transcript
                 1hej C 557 TGSCSVSAVRGEEWADRFNVTYSVSGSSSWVVTLGLNGGQSVQSSWNAALTGSSGTVTARPNGSGNSFGVTFYKNGSSATPGATCATG 644
                                   566       576       586       596       606       616       626       636        

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  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (1, 1)

NMR Structure

(-) CATH Domains  (1, 1)

NMR Structure
(-)
Class: Mainly Beta (13760)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 1HEJ)

(-) Gene Ontology  (12, 12)

NMR Structure(hide GO term definitions)
Chain C   (XYND_CELFI | P54865)
molecular function
    GO:0030246    carbohydrate binding    Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
    GO:0003824    catalytic activity    Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
    GO:0031176    endo-1,4-beta-xylanase activity    Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
    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:0016810    hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds    Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
    GO:0016798    hydrolase activity, acting on glycosyl bonds    Catalysis of the hydrolysis of any glycosyl bond.
    GO:0004553    hydrolase activity, hydrolyzing O-glycosyl compounds    Catalysis of the hydrolysis of any O-glycosyl bond.
    GO:0030247    polysaccharide binding    Interacting selectively and non-covalently with any polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
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: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.

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/Swiss-Prot
        XYND_CELFI | P548651e5b 1e5c 1heh 1xbd 2xbd

(-) Related Entries Specified in the PDB File

1e5b INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT
1e5c INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT
1heh C-TERMINAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE 11A (MINIMIZED AVERAGE STRUCTURE)
1xbd INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, 5 STRUCTURES
2xbd INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, MINIMIZED AVERAGE STRUCTURE