Journal
BIOCHEMISTRY
Volume 47, Issue 37, Pages 9715-9717Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi8010779
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Funding
- NIGMS NIH HHS [U54 GM074958, U54-GM074958] Funding Source: Medline
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Escherichia coli Spr is a membrane-anchored cell wall hydrolase. The solution NMR structure of the C-terminal NlpC/P60 domain of E. coli Spr described here reveals that the protein adopts a papain-like alpha+beta fold and identifies a substrate-binding cleft featuring several highly conserved residues. The active site features a novel Cys-His-His catalytic triad that appears to be a unique structural signature of this cysteine peptidase family. Moreover, the relative orientation of these catalytic residues is similar to that observed in the analogous Ser-His-His triad, a variant of the classic Ser-His-Asp charge relay system, suggesting the convergent evolution of a catalytic mechanism in quite distinct peptidase families.
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