4GJJ

Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with D-allopyranose

4GJJ の概要

• エントリーDOI: 10.2210/pdb4gjj/pdb
• 関連するPDBエントリー: 2HCV 2I57 4GJI
• 分子名称: L-rhamnose isomerase, MANGANESE (II) ION, D-ALLOSE, ... (5 entities in total)
• 機能のキーワード: tim barrel, isomerase, sugar binding, metal binding
• 由来する生物種: Pseudomonas stutzeri
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 193192.28

構造登録者

Yoshida, H.,Kamitori, S. (登録日: 2012-08-09, 公開日: 2012-12-12, 最終更新日: 2023-11-08)

主引用文献

Yoshida, H.,Yoshihara, A.,Teraoka, M.,Yamashita, S.,Izumori, K.,Kamitori, S.
Structure of l-rhamnose isomerase in complex with l-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site.
FEBS Open Bio, 3:35-40, 2013

PubMed Abstract: l-Rhamnose isomerase (l-RhI) catalyzes the reversible isomerization of l-rhamnose to l-rhamnulose. Previously determined X-ray structures of l-RhI showed a hydride-shift mechanism for the isomerization of substrates in a linear form, but the mechanism for opening of the sugar-ring is still unclear. To elucidate this mechanism, we determined X-ray structures of a mutant l-RhI in complex with l-rhamnopyranose and d-allopyranose. Results suggest that a catalytic water molecule, which acts as an acid/base catalyst in the isomerization reaction, is likely to be involved in pyranose-ring opening, and that a newly found substrate sub-binding site in the vicinity of the catalytic site may recognize different anomers of substrates.

PubMed: 23772372
DOI: 10.1016/j.fob.2012.11.008

実験手法

X-RAY DIFFRACTION (2.38 Å)