1SLX

RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; ZINC-BOUND

1SLX の概要

• エントリーDOI: 10.2210/pdb1slx/pdb
• 分子名称: ECOTIN, ANIONIC TRYPSIN, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: serine protease, inhibitor, complex, metal binding sites, protein engineering, protease-substrate interactions, metalloproteins, complex (serine protease-inhibitor) complex, complex (serine protease/inhibitor)
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Periplasm: P23827; Secreted, extracellular space: P00763
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40200.02

構造登録者

Brinen, L.S.,Fletterick, R.J. (登録日: 1996-02-07, 公開日: 1996-07-11, 最終更新日: 2024-11-20)

主引用文献

Brinen, L.S.,Willett, W.S.,Craik, C.S.,Fletterick, R.J.
X-ray structures of a designed binding site in trypsin show metal-dependent geometry.
Biochemistry, 35:5999-6009, 1996

PubMed Abstract: The three-dimensional structures of complexes of trypsin N143H, E151H bound to ecotin A86H are determined at 2.0 A resolution via X-ray crystallography in the absence and presence of the transition metals Zn2+, Ni2+, and Cu2+. The binding site for these transition metals was constructed by substitution of key amino acids with histidine at the trypsin-ecotin interface in the S2'/P2' pocket. Three histidine side chains, two on trypsin at positions 143 and 151 and one on ecotin at position 86, anchor the metals and provide extended catalytic recognition for substrates with His in the P2' pocket. Comparisons of the three-dimensional structures show the different geometries that result upon the binding of metal in the engineered tridentate site and suggest a structural basis for the kinetics of the metal-regulated catalysis. Of the three metals, the binding of zinc results in the most favorable binding geometry, not dissimilar to those observed in naturally occurring zinc binding proteins.

PubMed: 8634241
DOI: 10.1021/bi9530200

実験手法

X-RAY DIFFRACTION (2.2 Å)