2H6T

Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A

2H6T の概要

• エントリーDOI: 10.2210/pdb2h6t/pdb
• 関連するPDBエントリー: 2H6S
• 関連するBIRD辞書のPRD_ID: PRD_000557
• 分子名称: Candidapepsin-3, pepstatin A, ZINC ION, ... (4 entities in total)
• 機能のキーワード: aspartic proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Candida albicans; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37293.13

構造登録者

Ruge, E.,Borelli, C.,Maskos, K.,Huber, R. (登録日: 2006-06-01, 公開日: 2007-06-12, 最終更新日: 2024-10-30)

主引用文献

Borelli, C.,Ruge, E.,Schaller, M.,Monod, M.,Korting, H.C.,Huber, R.,Maskos, K.
The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A.
Proteins, 68:738-748, 2007

PubMed Abstract: The family of secreted aspartic proteinases (Sap) encoded by 10 SAP genes is an important virulence factor during Candida albicans (C. albicans) infections. Antagonists to Saps could be envisioned to help prevent or treat candidosis in immunocompromised patients. The knowledge of several Sap structures is crucial for inhibitor design; only the structure of Sap2 is known. We report the 1.9 and 2.2 A resolution X-ray crystal structures of Sap3 in a stable complex with pepstatin A and in the absence of an inhibitor, shedding further light on the enzyme inhibitor binding. Inhibitor binding causes active site closure by the movement of a flap segment. Comparison of the structures of Sap3 and Sap2 identifies elements responsible for the specificity of each isoenzyme.

PubMed: 17510964
DOI: 10.1002/prot.21425

実験手法

X-RAY DIFFRACTION (1.9 Å)