Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: Structural evidence for a novel cysteine peptidase catalytic triad

James M. Aramini, Paolo Rossi, Yuanpeng J. Huang, Li Zhao, Mei Jiang, Melissa Maglaqui, Rong Xiao, Jessica Locke, Rajesh Nair, Burkhard Rost, Thomas B. Acton, Masayori Inouye, Gaetano T. Montelione

Research output: Contribution to journalArticle

53 Scopus citations

Abstract

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 α+β 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.

Original languageEnglish (US)
Pages (from-to)9715-9717
Number of pages3
JournalBiochemistry
Volume47
Issue number37
DOIs
StatePublished - Sep 16 2008

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