3URI

Endothiapepsin-DB5 complex.

3URI の概要

• エントリーDOI: 10.2210/pdb3uri/pdb
• 関連するPDBエントリー: 3URJ 3URL
• 関連するBIRD辞書のPRD_ID: PRD_000855
• 分子名称: Endothiapepsin, DB5 peptide (3 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, aspartic proteinase mechanism, transition state analogue., hydrolase/hydrolase inhibitor
• 由来する生物種: Cryphonectria parasitica (Chesnut blight fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34861.11

構造登録者

Bailey, D.,Sanz-Aparicio, J.,Albert, A.,Cooper, J.B. (登録日: 2011-11-22, 公開日: 2012-04-18, 最終更新日: 2023-11-15)

主引用文献

Bailey, D.,Carpenter, E.P.,Coker, A.,Coker, S.,Read, J.,Jones, A.T.,Erskine, P.,Aguilar, C.F.,Badasso, M.,Toldo, L.,Rippmann, F.,Sanz-Aparicio, J.,Albert, A.,Blundell, T.L.,Roberts, N.B.,Wood, S.P.,Cooper, J.B.
An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.
Acta Crystallogr.,Sect.D, 68:541-552, 2012

PubMed Abstract: The analysis reported here describes detailed structural studies of endothiapepsin (the aspartic proteinase from Endothia parasitica), with and without bound inhibitors, and human pepsin 3b. Comparison of multiple crystal structures of members of the aspartic proteinase family has revealed small but significant differences in domain orientation in different crystal forms. In this paper, it is shown that these differences in domain orientation do not necessarily correlate with the presence or absence of bound inhibitors, but appear to stem at least partly from crystal contacts mediated by sulfate ions. However, since the same inherent flexibility of the structure is observed for other enzymes in this family such as human pepsin, the native structure of which is also reported here, the observed domain movements may well have implications for the mechanism of catalysis.

PubMed: 22525752
DOI: 10.1107/S0907444912004817

実験手法

X-RAY DIFFRACTION (2.1 Å)