Pro42 and Val45 of staphylokinase modulate intermolecular interactions of His43-Tyr44 pair and specificity of staphylokinase-plasmin activator complex

被引：8

作者：

Singh, Satish ^{[1
]}

Ashish ^{[1
]}

Dikshit, Kanak L. ^{[1
]}

机构：

[1] CSIR, Inst Microbial Technol, Sect 39 A, Chandigarh 160036, India

来源：

FEBS LETTERS | 2012年 / 586卷 / 06期

关键词：

Staphylokinase; Plasminogen activation; Molecular modeling; Site-directed mutagenesis; Enzyme-substrate complex; Protein-protein interaction; RECOMBINANT STAPHYLOKINASE; MYOCARDIAL-INFARCTION; SUBSTRATE COMPLEX; CRYSTAL-STRUCTURE; STREPTOKINASE; MECHANISM; REGION; MODEL;

D O I：

10.1016/j.febslet.2012.01.046

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Staphylokinase (SAK) forms a 1:1 stoichiometric complex with plasmin (Pm) and changes its substrate specificity to create a plasminogen (Pg) activator complex. The His(43)-Tyr(44) pair of SAK resides within the active site cleft of the partner Pm and generates intermolecular contacts to confer Pg activator ability to the SAK-Pm bimolecular complex. Site-directed mutagenesis and molecular modeling studies unravelled that mutation at 42nd or 45th positions of SAK specifically disrupts cation-pi interaction of His(43) with Trp(215) of partner Pm within the active site, whereas pi-pi interaction of Tyr(44) with Trp(215) remain energetically favoured. Structured summary of protein interactions: Pg binds to SAK by surface plasmon resonance (View Interaction: 1, 2, 3) SAK enzymaticly reacts Pg by enzymatic study (View Interaction: 1, 2, 3, 4, 5) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：653 / 658

页数：6

共 29 条

[1] Identification of a New Exosite Involved in Catalytic Turnover by the Streptokinase-Plasmin Activator Complex during Human Plasminogen Activation [J].