3ENV

Substrate and inhibitor complexes of ribose 5-phosphate isomerase from Vibrio vulnificus YJ016

3ENV の概要

• エントリーDOI: 10.2210/pdb3env/pdb
• 関連するPDBエントリー: 3ENW
• 分子名称: Ribose-5-phosphate isomerase A, 5-O-phosphono-beta-D-arabinofuranose (3 entities in total)
• 機能のキーワード: ribose 5-phosphate, arabinose 5-phosphate, isomerase
• 由来する生物種: Vibrio vulnificus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49804.65

構造登録者

Min, K.,Kwon, T.H.,Kim, T.G. (登録日: 2008-09-26, 公開日: 2009-09-29, 最終更新日: 2023-11-01)

主引用文献

Kim, T.G.,Kwon, T.H.,Min, K.,Dong, M.S.,Park, Y.I.,Ban, C.
Crystal structures of substrate and inhibitor complexes of ribose 5-phosphate isomerase A from Vibrio vulnificus YJ016
Mol.Cells, 27:99-103, 2009

PubMed Abstract: Ribose-5-phosphate isomerase A (RpiA) plays an important role in interconverting between ribose-5-phosphate (R5P) and ribulose-5-phosphate in the pentose phosphate pathway and the Calvin cycle. We have determined the crystal structures of the open form RpiA from Vibrio vulnificus YJ106 (VvRpiA) in complex with the R5P and the closed form with arabinose-5-phosphate (A5P) in parallel with the apo VvRpiA at 2.0 A resolution. VvRpiA is highly similar to Eschericihia coliRpiA, and the VvRpiA-R5P complex strongly resembles the E. coli RpiA-A5P complex. Interestingly, unlike the E. coli RpiA-A5P complex, the position of A5P in the VvRpiA-A5P complex reveals a different position than the R5P binding mode. VvRpiA-A5P has a sugar ring inside the binding pocket and a phosphate group outside the binding pocket: By contrast, the sugar ring of A5P interacts with the Asp4, Lys7, Ser30, Asp118, and Lys121 residues; the phosphate group of A5P interacts with two water molecules, W51 and W82.

PubMed: 19214439
DOI: 10.1007/s10059-009-0010-6

実験手法

X-RAY DIFFRACTION (2 Å)