1V5X

Crystal structure of Phosphoribosyl anthranilate isomerase from Thermus Thermophilus

1V5X の概要

• エントリーDOI: 10.2210/pdb1v5x/pdb
• 分子名称: Phosphoribosylanthranilate isomerase (2 entities in total)
• 機能のキーワード: isomerase, alpha-beta barrel, trpf, phosphoribosyl anthranilate isomerase, riken structural genomics/proteomics initiative, rsgi, structural genomics
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43954.92

構造登録者

Taka, J.,Kunishima, N.,Yutani, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-11-26, 公開日: 2003-12-23, 最終更新日: 2023-10-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)