PDBsum entry 1v5x

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Isomerase PDB id
Protein chains
200 a.a. *
Waters ×301
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Crystal structure of phosphoribosyl anthranilate isomerase from thermus thermophilus
Structure: Phosphoribosylanthranilate isomerase. Chain: a, b. Synonym: pra isomerase. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
2.00Å     R-factor:   0.262     R-free:   0.296
Authors: J.Taka,N.Kunishima,K.Yutani,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: J.Taka et al. (2005). Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments. J Biochem, 137, 569-578. PubMed id: 15944409 DOI: 10.1093/jb/mvi075
26-Nov-03     Release date:   23-Dec-03    
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Protein chains
Pfam   ArchSchema ?
P83825  (P83825_THETH) -  N-(5'-phosphoribosyl)anthranilate isomerase
203 a.a.
200 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Phosphoribosylanthranilate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Tryptophan Biosynthesis
      Reaction: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate
= 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     3 terms  


    Added reference    
DOI no: 10.1093/jb/mvi075 J Biochem 137:569-578 (2005)
PubMed id: 15944409  
Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments.
J.Taka, K.Ogasahara, J.Jeyakanthan, N.Kunishima, C.Kuroishi, M.Sugahara, S.Yokoyama, K.Yutani.
The crystal structure of phosphoribosyl anthranilate isomerase (PRAI) from Thermus thermophilus HB8 (TtPRAI) was solved at 2.0 A resolution. The overall structure of TtPRAI with a dimeric structure was quite similar to that of PRAI from Thermotoga maritima (TmPRAI). In order to elucidate the stabilization mechanism of TtPRAI, its physicochemical properties were examined using DSC, CD, and analytical centrifugation at various pHs in relation to the association-dissociation of the subunits. Based on the experimental results for TtPRAI and the structural information on TtPRAI and TmPRAI, we found that: (i) the denaturation of TtPRAI at acidic pH is correlated with the dissociation of its dimeric form; (ii) the hydrophobic interaction of TtPRAI in the monomer structure is slightly greater than that of TmPRAI, but dimer interface of the TmPRAI is remarkably greater; (iii) the contributions of hydrogen bonds and ion bonds to the stability are similar to each other; and (iv) destabilization due to the presence of cavities in TtPRAI is greater than that of TmPRAI in both the monomer and dimer structures.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21197556 D.Shen, X.Xu, H.Wu, L.Peng, Y.Zhang, J.Song, and Q.Su (2011).
Metal ion binding to anticoagulation factor II from the venom of Agkistrodon acutus: stabilization of the structure and regulation of the binding affinity to activated coagulation factor X.
  J Biol Inorg Chem, 16, 523-537.  
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