Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease

Title
Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease
Author(s)
김도연[김도연]Boi Hoa San[Boi Hoa San]모상현[모상현]박혜진[박혜진]김동영이상호[이상호]김경규[김경규]
Keywords
PYROCOCCUS-HORIKOSHII; CRYSTAL-STRUCTURE; TRICORN PROTEASE; AMINOPEPTIDASE; DEGRADATION; PROTEOLYSIS; COMPLEX; ARCHAEA; SYSTEM
Issue Date
201001
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.391, no.1, pp.431 - 436
Abstract
Regulated cytosolic proteolysis is one of the key cellular processes ensuring proper functioning of a cell M42 family proteases show a broad spectrum of substrate specificities, but the structural basis for such diversity of the substrate specificities is lagging behind biochemical data Here we report the crystal structure of PepA from Streptococcus pneumoniae, a glutamyl aminopeptidase belonging to M42 family (SpPepA) We found that Arg-257 in the Substrate binding pocket is strategically positioned so that Arg-257 can make electrostatic interactions with the acidic residue of a substrate at its N-terminus Structural comparison of the Substrate binding pocket of the M42 family proteases, along with the structure-based multiple sequence alignment, argues that the appropriate electrostatic interactions contribute to the selective substrate specificity of SpPepA (C) 2009 Elsevier Inc All rights reserved
URI
http://hdl.handle.net/YU.REPOSITORY/22994http://dx.doi.org/10.1016/j.bbrc.2009.11.075
ISSN
0006-291X
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약학대학 > 약학부 > Articles
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