1J71

Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.

1J71 の概要

• エントリーDOI: 10.2210/pdb1j71/pdb
• 関連するPDBエントリー: 1EAG 1ZAP
• 分子名称: Aspartic proteinase, Tetrapeptide Thr-Ile-Thr-Ser, ETHANOL, ... (4 entities in total)
• 機能のキーワード: candida tropicalis aspartic protease, sapt1, hydrolase
• 由来する生物種: Candida tropicalis; 詳細
• 細胞内の位置: Secreted: Q00663
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36651.13

構造登録者

Symersky, J.,Monod, M.,Foundling, S.I. (登録日: 2001-05-15, 公開日: 2001-05-23, 最終更新日: 2024-10-16)

主引用文献

Symersky, J.,Monod, M.,Foundling, S.I.
High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast.
Biochemistry, 36:12700-12710, 1997

PubMed Abstract: The crystal structure of the secreted aspartic proteinase from Candida tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The classic aspartic proteinase bilobal structure and domain topology is conserved in SAPT, with the substrate binding cleft situated between the two domains. Structural comparisons made with pepsin indicate that insertions and deletions in the primary sequence modify the SAPT structure to create a more spacious substrate binding cleft with altered specificity. An unexpected tetrapeptide has been found to occupy binding sites S1'-S3', and this suggests the order of release of peptide products in the catalytic mechanism of these enzymes. Structural features are considered with regard to previous substrate specificity data.

PubMed: 9335526
DOI: 10.1021/bi970613x

実験手法

X-RAY DIFFRACTION (1.8 Å)