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PDBsum entry 2r7l

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protein ligands metals links
Ligase PDB id
2r7l
Jmol
Contents
Protein chain
355 a.a. *
Ligands
SO4
ATP
AMZ
Metals
_CL ×2
Waters ×128
* Residue conservation analysis
PDB id:
2r7l
Name: Ligase
Title: Crystal structure of faicar synthetase (purp) from m. Jannaschii complexed with atp and aicar
Structure: 5-formaminoimidazole-4-carboxamide-1-(beta)-d- ribofuranosyl 5'-monophosphate synthetase. Chain: a. Synonym: 5-aminoimidazole-4-carboxamide-1-beta-d- ribofuranosyl 5'-monophosphate-formate ligase. Engineered: yes
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: purp. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: b834(de3).
Resolution:
2.10Å     R-factor:   0.211     R-free:   0.260
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
Date:
09-Sep-07     Release date:   04-Dec-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q57600  (PURP_METJA) -  5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase
Seq:
Struc:
361 a.a.
355 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.4.23  - 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
ATP
+ formate
+ 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
= ADP
+ phosphate
+ 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     IMP biosynthetic process   2 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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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