| Literature DB >> 19217401 |
Qingping Xu1, Sebastian Sudek, Daniel McMullan, Mitchell D Miller, Bernhard Geierstanger, David H Jones, S Sri Krishna, Glen Spraggon, Badry Bursalay, Polat Abdubek, Claire Acosta, Eileen Ambing, Tamara Astakhova, Herbert L Axelrod, Dennis Carlton, Jonathan Caruthers, Hsiu-Ju Chiu, Thomas Clayton, Marc C Deller, Lian Duan, Ylva Elias, Marc-André Elsliger, Julie Feuerhelm, Slawomir K Grzechnik, Joanna Hale, Gye Won Han, Justin Haugen, Lukasz Jaroszewski, Kevin K Jin, Heath E Klock, Mark W Knuth, Piotr Kozbial, Abhinav Kumar, David Marciano, Andrew T Morse, Edward Nigoghossian, Linda Okach, Silvya Oommachen, Jessica Paulsen, Ron Reyes, Christopher L Rife, Christina V Trout, Henry van den Bedem, Dana Weekes, Aprilfawn White, Guenter Wolf, Chloe Zubieta, Keith O Hodgson, John Wooley, Ashley M Deacon, Adam Godzik, Scott A Lesley, Ian A Wilson.
Abstract
The crystal structures of two homologous endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme were determined at 1.05 and 1.60 A resolution, respectively, and contain a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NlpC/P60 (or CHAP) cysteine peptidase domain. The NlpC/P60 domain is a primitive, papain-like peptidase in the CA clan of cysteine peptidases with a Cys126/His176/His188 catalytic triad and a conserved catalytic core. We deduced from structure and sequence analysis, and then experimentally, that these two proteins act as gamma-D-glutamyl-L-diamino acid endopeptidases (EC 3.4.22.-). The active site is located near the interface between the SH3b and NlpC/P60 domains, where the SH3b domain may help define substrate specificity, instead of functioning as a targeting domain, so that only muropeptides with an N-terminal L-alanine can bind to the active site.Entities:
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Year: 2009 PMID： 19217401 PMCID： PMC2667786 DOI： 10.1016/j.str.2008.12.008
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006