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

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Pro42 and Val45 of staphylokinase modulate intermolecular interactions of His43-Tyr44 pair and specificity of staphylokinase-plasmin activator complex.
 
Creator Singh, Satish
Ganguly, Ashish
Dikshit, Kanak L
 
Subject QR Microbiology
 
Description 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.
 
Publisher Elsevier Science
 
Date 2012-03-23
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/1264/1/dikshit2012.pdf
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
 
Relation http://www.sciencedirect.com/science/article/pii/S0014579312000798
http://crdd.osdd.net/open/1264/