1SMP

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN SERRATIA MARCESCENS METALLO-PROTEASE AND AN INHIBITOR FROM ERWINIA CHRYSANTHEMI

1SMP の概要

• エントリーDOI: 10.2210/pdb1smp/pdb
• 分子名称: SERRATIA METALLO PROTEINASE, ERWINIA CHRYSANTHEMI INHIBITOR, ZINC ION, ... (5 entities in total)
• 機能のキーワード: complex (metalloprotease-inhibitor), complex (metalloprotease-inhibitor) complex, complex (metalloprotease/inhibitor)
• 由来する生物種: Serratia marcescens; 詳細
• 細胞内の位置: Secreted: P23694; Periplasm: P18958
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61805.58

構造登録者

Baumann, U.,Bauer, M.,Letoffe, S.,Delepelaire, P.,Wandersman, C. (登録日: 1995-01-13, 公開日: 1996-04-03, 最終更新日: 2024-11-13)

主引用文献

Baumann, U.,Bauer, M.,Letoffe, S.,Delepelaire, P.,Wandersman, C.
Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.
J.Mol.Biol., 248:653-661, 1995

PubMed Abstract: The crystal structure of the complex between the 50 kDa metallo-endoproteinase from Serratia marcescens (SMP), a member of the metzincin superfamily, and an inhibitor from Erwinia chrysanthemi (Inh) was solved by molecular replacement using the known structure of SMP, and refined at 2.30 A resolution to a crystallographic R-factor of 0.195. The E. chrysanthemi inhibitor folds into a compact eight-stranded antiparallel beta-barrel of simple up-down topology such as is found for members of the retinol binding protein family. It mainly interacts with the protease via its five N-terminal residues, which insert into the active site cleft, occupying the S' sites. The first N-terminal residue, SerI1, is partially cleaved off by the protease, while SerI2 makes a hydrogen bond with the catalytically active glutamic acid, Glu177, of the protease. Further interactions are made between one face of the inhibitor formed by the strands s3, s4 and s5 and the protease segment 218 to 228, which is located immediately after the characteristic "Met-turn" of the metzincins.

PubMed: 7752231
DOI: 10.1006/jmbi.1995.0249

実験手法

X-RAY DIFFRACTION (2.3 Å)