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(-) Description

Title :  SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE FROM BACILLUS SUBTILIS
 
Authors :  H. Xu, B. Xia, C. Jin
Date :  21 Apr 05  (Deposition) - 28 Mar 06  (Release) - 24 Feb 09  (Revision)
Method :  SOLUTION NMR
Resolution :  NOT APPLICABLE
Chains :  NMR Structure  :  A  (20x)
Keywords :  Alpha/Beta, Four-Stranded Parallel Beta Sheet, Structural Genomics, Hydrolase (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  H. Xu, B. Xia, C. Jin
Solution Structure Of A Low-Molecular-Weight Protein Tyrosine Phosphatase From Bacillus Subtilis
J. Bacteriol. V. 188 1509 2006
PubMed-ID: 16452434  |  Reference-DOI: 10.1128/JB.188.4.1509-1517.2006
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - PUTATIVE LOW MOLECULAR WEIGHT PROTEIN-TYROSINE- PHOSPHATASE YWLE
    Chains: A
    EC Number: 3.1.3.48
    Engineered: YES
    Expression System: ESCHERICHIA COLI BL21(DE3)
    Expression System Plasmid: PET21
    Expression System Strain: BL21(DE3)
    Expression System Taxid: 469008
    Expression System Vector Type: PLASMID
    Organism Scientific: BACILLUS SUBTILIS
    Organism Taxid: 1423
    Synonym: LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE

 Structural Features

(-) Chains, Units

  
NMR Structure (20x): 

Summary Information (see also Sequences/Alignments below)

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

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

(-) Sites  (0, 0)

(no "Site" information available for 1ZGG)

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 1ZGG)

(-) Cis Peptide Bonds  (0, 0)

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

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

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

(-) PROSITE Motifs  (0, 0)

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(-) Exons   (0, 0)

(no "Exon" information available for 1ZGG)

(-) 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
(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:150
 aligned with PAP_BACSU | P39155 from UniProtKB/Swiss-Prot  Length:150

    Alignment length:150
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150
            PAP_BACSU     1 MDIIFVCTGNTCRSPMAEALFKSIAEREGLNVNVRSAGVFASPNGKATPHAVEALFEKHIALNHVSSPLTEELMESADLVLAMTHQHKQIIASQFGRYRDKVFTLKEYVTGSHGDVLDPFGGSIDIYKQTRDELEELLRQLAKQLKKDRR 150
               SCOP domains d1zgga_ A: automated matches                                                                                                                           SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author .eeeee......hhhhhhhhhhhhhhhhh...eeeee............hhhhhhhhh...........hhhhhhhh.eeee.hhhhhhhhhhhhh.hhh.eee.hhhhhh...........hhhhhhhhhhhhhhhhhhhhhhhh.... Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------ PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                 1zgg A   1 MDIIFVCTGNTCRSPMAEALFKSIAEREGLNVNVRSAGVFASPNGKATPHAVEALFEKHIALNHVSSPLTEELMESADLVLAMTHQHKQIIASQFGRYRDKVFTLKEYVTGSHGDVLDPFGGSIDIYKQTRDELEELLRQLAKQLKKDRR 150
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150
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  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  (1, 1)

NMR Structure
(-)
Class: Alpha and beta proteins (a/b) (23833)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 1ZGG)

(-) Pfam Domains  (0, 0)

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

(-) Gene Ontology  (5, 5)

NMR Structure(hide GO term definitions)
Chain A   (PAP_BACSU | P39155)
molecular function
    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:0004721    phosphoprotein phosphatase activity    Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
    GO:0004725    protein tyrosine phosphatase activity    Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
biological process
    GO:0035335    peptidyl-tyrosine dephosphorylation    The removal of phosphoric residues from peptidyl-O-phospho-tyrosine to form peptidyl-tyrosine.
    GO:0006470    protein dephosphorylation    The process of removing one or more phosphoric residues from a protein.

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 Related Entries

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        PAP_BACSU | P39155: 4eti 4etn 4kk3 4kk4

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