3ER5

THE ACTIVE SITE OF ASPARTIC PROTEINASES

3ER5 の概要

• エントリーDOI: 10.2210/pdb3er5/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000430
• 分子名称: ENDOTHIAPEPSIN, H-189 (3 entities in total)
• 機能のキーワード: acid proteinase, hydrolase-hydrolase inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Cryphonectria parasitica
• 細胞内の位置: Secreted: P01017
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35086.39

構造登録者

Bailey, D.,Veerapandian, B.,Cooper, J.,Szelke, M.,Blundell, T.L. (登録日: 1991-01-05, 公開日: 1991-04-15, 最終更新日: 2024-10-23)

主引用文献

Bailey, D.,Cooper, J.B.,Veerapandian, B.,Blundell, T.L.,Atrash, B.,Jones, D.M.,Szelke, M.
X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
Biochem.J., 289 ( Pt 2):363-371, 1993

PubMed Abstract: H-189, a synthetic human renin inhibitor, and pepstatin A, a naturally occurring inhibitor of aspartic proteinases, have been co-crystallized with the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6). H-189 [Pro-His-Pro-Phe-His-Sta-(statyl)-Val-Ile-His-Lys] is an analogue of human angiotensinogen. Pepstatin A [Iva(isovaleryl)-Val-Val-Sta-Ala-Sta] is a blocked pentapeptide which inhibits many aspartic proteinases. The structures of the complexes have been determined by X-ray diffraction and refined to crystallographic R-factors of 0.15 and 0.16 at resolutions of 0.18 nm (1.8 A) and 0.2 nm (2.0 A) respectively. H-189 is in an extended conformation, in which the statine residue is a dipeptide analogue of P1 and P'1 as indicated by the conformation and network of contacts and hydrogen bonds. Pepstatin A has an extended conformation to the P'2 alanine residue, but the leucyl side chain of the terminal statine residue binds back into the S'1 subsite, and an inverse gamma-turn occurs between P'1 and P'3. The hydroxy moiety of the statine at P1 in both complexes displaces the solvent molecule that hydrogen-bonds with the catalytic aspartate residues (32 and 215) in the native enzyme. Solvent molecules originally present in the native structure at the active site are displaced on inhibitor binding (12 when pepstatin A binds; 16 when H-189 binds).

PubMed: 8424781

実験手法

X-RAY DIFFRACTION (1.8 Å)