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

Singh, Satish and Ganguly, Ashish and Dikshit, Kanak L (2012) Pro42 and Val45 of staphylokinase modulate intermolecular interactions of His43-Tyr44 pair and specificity of staphylokinase-plasmin activator complex. FEBS letters, 586 (6). pp. 653-8. ISSN 1873-3468

PDF dikshit2012.pdf - Published Version Restricted to Registered users only Download (715Kb) | Request a copy

Abstract

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.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Elsevier Science.
Uncontrolled Keywords:	Staphylokinase; Plasminogen activation;Molecular modeling; Site-directed mutagenesis; Enzyme–substrate complex; Protein–protein interaction.
Subjects:	Q Science > QR Microbiology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	28 Jan 2013 06:37
Last Modified:	22 Jul 2015 03:38
URI:	http://crdd.osdd.net/open/id/eprint/1264

Actions (login required)

View Item