Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease
- Authors
- Kim, D[Kim, Doyoun]; San, BH[San, Boi Hoa]; Moh, SH[Moh, Sang Hyun]; Park, H[Park, Hyejin]; Kim, DY[Kim, Dong Young]; Lee, S[Lee, Sangho]; Kim, KK[Kim, Kyeong Kyu]
- Issue Date
- 1-Jan-2010
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Glutamyl aminopeptidase; PepA; Tetrahedral aminopeptidase; Substrate specificity; M42 family protease; Streptococcus pneumoniae
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.391, no.1, pp.431 - 436
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 391
- Number
- 1
- Start Page
- 431
- End Page
- 436
- URI
- https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/75138
- DOI
- 10.1016/j.bbrc.2009.11.075
- ISSN
- 0006-291X
- 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
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- Appears in
Collections - Science > Department of Biological Science > 1. Journal Articles
- Medicine > Department of Medicine > 1. Journal Articles
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