PDBsum entry 1v5x

Isomerase

PDB id: 1v5x

Contents

Protein chains

200 a.a. *

Waters ×301

* Residue conservation analysis

PDB id:

1v5x

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)

Resolution:

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 (tokyo), 137, 569-578. PubMed id: 15944409

Date:

26-Nov-03 Release date: 23-Dec-03

Protein chains

P83825  (P83825_THETH) -  N-(5'-phosphoribosyl)anthranilate isomerase from Thermus thermophilus

Seq: 203 a.a.

Struc: 200 a.a.

Enzyme reactions

• Enzyme class: E.C.5.3.1.24 - phosphoribosylanthranilate isomerase.
• Pathway: Tryptophan Biosynthesis
• Reaction: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

J Biochem (tokyo) 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.

ABSTRACT

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.