Journal
STRUCTURE
Volume 17, Issue 2, Pages 303-313Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.12.008
Keywords
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Funding
- National Institute of General Medical Sciences (NIGMS) Protein Structure Initiative [U54 GM074898]
- U.S. Department of Energy [DE-AC03-76SF00098]
- Lawrence Berkeley National Laboratory
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The crystal structures of two homologous endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme were determined at 1.05 and 1.60 angstrom resolution, respectively, and contain a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NIpC/P60 (or CHAP) cysteine peptidase domain. The NIpC/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.
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