4XHC

rhamnosidase from Klebsiella oxytoca with rhamnose bound

4XHC の概要

• エントリーDOI: 10.2210/pdb4xhc/pdb
• 分子名称: Alpha-L-rhamnosidase, alpha-L-rhamnopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Klebsiella oxytoca
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 124125.85

構造登録者

O'Neill, E.O.,Stevenson, C.E.M.,Patterson, M.J.,Rejzek, M.,Chauvin, A.,Lawson, D.M.,Field, R.A. (登録日: 2015-01-05, 公開日: 2015-04-15, 最終更新日: 2024-05-08)

主引用文献

O'Neill, E.C.,Stevenson, C.E.,Paterson, M.J.,Rejzek, M.,Chauvin, A.L.,Lawson, D.M.,Field, R.A.
Crystal structure of a novel two domain GH78 family alpha-rhamnosidase from Klebsiella oxytoca with rhamnose bound.
Proteins, 83:1742-1749, 2015

PubMed Abstract: The crystal structure of the GH78 family α-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 Å resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays α-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function.

PubMed: 25846411
DOI: 10.1002/prot.24807

実験手法

X-RAY DIFFRACTION (2.7 Å)