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PDBsum entry 2y88

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Isomerase PDB id
2y88
Jmol
Contents
Protein chain
244 a.a. *
Ligands
2ER
Waters ×394
* Residue conservation analysis
PDB id:
2y88
Name: Isomerase
Title: Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase (variant d11n) with bound prfar
Structure: Phosphoribosyl isomerase a. Chain: a. Synonym: n-(5'-phosphoribosyl)anthranilate isomerase, 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino) methyliden imidazole-4-carboxamide isomerase, phosphoribosylformimino-5-aminoimidazole carboxamide ribot isomerase, prai. Engineered: yes. Mutation: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.33Å     R-factor:   0.140     R-free:   0.183
Authors: J.Kuper,A.V.Due,A.Geerlof,M.Wilmanns
Key ref: A.V.Due et al. (2011). Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis. Proc Natl Acad Sci U S A, 108, 3554-3559. PubMed id: 21321225
Date:
03-Feb-11     Release date:   02-Mar-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam  
P9WMM5  (HIS4_MYCTU) -  Phosphoribosyl isomerase A
Seq:
Struc:
244 a.a.
244 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: E.C.5.3.1.16  - 1-(5-phosphoribosyl)-5-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Histidine Biosynthesis (early stages)
      Reaction: 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1- deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide
   Enzyme class 3: E.C.5.3.1.24  - Phosphoribosylanthranilate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate
N-(5-phospho-beta-D-ribosyl)anthranilate
Bound ligand (Het Group name = 2ER)
matches with 42.86% similarity
= 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    Added reference    
 
 
Proc Natl Acad Sci U S A 108:3554-3559 (2011)
PubMed id: 21321225  
 
 
Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis.
A.V.Due, J.Kuper, A.Geerlof, J.P.von Kries, M.Wilmanns.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21983966 S.Fushinobu, H.Nishimasu, D.Hattori, H.J.Song, and T.Wakagi (2011).
Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase.
  Nature, 478, 538-541.
PDB code: 3r1m
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.