PDBsum entry 2r87

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Unknown function PDB id
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Protein chains
(+ 0 more) 334 a.a. *
ADP ×6
PO4 ×19
Waters ×541
* Residue conservation analysis
PDB id:
Name: Unknown function
Title: Crystal structure of purp from pyrococcus furiosus complexed with adp
Structure: Purp protein pf1517. Chain: a, b, c, d, e, f. Engineered: yes
Source: Pyrococcus furiosus. Organism_taxid: 2261. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
2.30Å     R-factor:   0.203     R-free:   0.244
Authors: Y.Zhang,R.H.White,S.E.Ealick
Key ref: Y.Zhang et al. (2008). Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii. Biochemistry, 47, 205-217. PubMed id: 18069798
10-Sep-07     Release date:   04-Dec-07    
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Protein chains
Pfam   ArchSchema ?
Q8U0R7  (PURP_PYRFU) -  5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase
334 a.a.
334 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Formate--phosphoribosylaminoimidazolecarboxamide ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + formate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = ADP + phosphate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide
+ formate
+ 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Bound ligand (Het Group name = ADP)
corresponds exactly
Bound ligand (Het Group name = PO4)
corresponds exactly
+ 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     purine nucleotide biosynthetic process   3 terms 
  Biochemical function     nucleotide binding     6 terms  


Biochemistry 47:205-217 (2008)
PubMed id: 18069798  
Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii.
Y.Zhang, R.H.White, S.E.Ealick.
Purine biosynthesis requires 10 enzymatic steps in higher organisms, while prokaryotes require an additional enzyme for step 6. In most organisms steps 9 and 10 are catalyzed by the purH gene product, a bifunctional enzyme with both 5-formaminoimidazole-4-carboxamide ribonucleotide (FAICAR) synthase and inosine monophosphate (IMP) cyclohydrolase activity. Recently it was discovered that Archaea utilize different enzymes to catalyze steps 9 and 10. An ATP-dependent FAICAR synthetase is encoded by the purP gene, and IMP cyclohydrolase is encoded by the purO gene. We have determined the X-ray crystal structures of FAICAR synthetase from Methanocaldococcus jannaschii complexed with various ligands, including the tertiary substrate complex and product complex. The enzyme belongs to the ATP grasp superfamily and is predicted to use a formyl phosphate intermediate formed by an ATP-dependent phosphorylation. In addition, we have determined the structures of a PurP orthologue from Pyrococcus furiosus, which is functionally unclassified, in three crystal forms. With approximately 50% sequence identity, P. furiosus PurP is structurally homologous to M. jannaschii PurP. A phylogenetic analysis was performed to explore the possible role of this functionally unclassified PurP.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18712276 Y.Zhang, M.Morar, and S.E.Ealick (2008).
Structural biology of the purine biosynthetic pathway.
  Cell Mol Life Sci, 65, 3699-3724.  
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