4YBF

Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 1.25 A Resolution

4YBF の概要

• エントリーDOI: 10.2210/pdb4ybf/pdb
• 分子名称: Candidapepsin-2, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: aspartic proteinase sapp2, hydrolase
• 由来する生物種: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35580.13

構造登録者

Dostal, J.,Hruskova-Heidingsfeldova, O.,Rezacova, P.,Brynda, J.,Mareckova, L.,Pichova, I. (登録日: 2015-02-18, 公開日: 2016-01-27, 最終更新日: 2024-11-20)

主引用文献

Dostal, J.,Pecina, A.,Hruskova-Heidingsfeldova, O.,Mareckova, L.,Pichova, I.,Rezacova, P.,Lepsik, M.,Brynda, J.
Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.
Acta Crystallogr.,Sect.D, 71:2494-2504, 2015

PubMed Abstract: The virulence of the Candida pathogens is enhanced by the production of secreted aspartic proteases, which therefore represent possible targets for drug design. Here, the crystal structure of the secreted aspartic protease Sapp2p from Candida parapsilosis was determined. Sapp2p was isolated from its natural source and crystallized in complex with pepstatin A, a classical aspartic protease inhibitor. The atomic resolution of 0.83 Å allowed the protonation states of the active-site residues to be inferred. A detailed comparison of the structure of Sapp2p with the structure of Sapp1p, the most abundant C. parapsilosis secreted aspartic protease, was performed. The analysis, which included advanced quantum-chemical interaction-energy calculations, uncovered molecular details that allowed the experimentally observed equipotent inhibition of both isoenzymes by pepstatin A to be rationalized.

PubMed: 26627656
DOI: 10.1107/S1399004715019392

実験手法

X-RAY DIFFRACTION (1.24 Å)