1V5X

Crystal structure of Phosphoribosyl anthranilate isomerase from Thermus Thermophilus

Summary for 1V5X

• Entry DOI: 10.2210/pdb1v5x/pdb
• Descriptor: Phosphoribosylanthranilate isomerase (2 entities in total)
• Functional Keywords: isomerase, alpha-beta barrel, trpf, phosphoribosyl anthranilate isomerase, riken structural genomics/proteomics initiative, rsgi, structural genomics
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 43954.92

Authors

Taka, J.,Kunishima, N.,Yutani, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-11-26, release date: 2003-12-23, Last modification date: 2023-10-25)

Primary citation

Taka, J.,Ogasahara, K.,Jeyakanthan, J.,Kunishima, N.,Kuroishi, C.,Sugahara, M.,Yokoyama, S.,Yutani, K.
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, 2005

PubMed 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.

PubMed: 15944409
DOI: 10.1093/jb/mvi075

Experimental method

X-RAY DIFFRACTION (2 Å)