2K1G: Solution NMR structure of lipoprotein spr from Escherichia coli K12. Northeast Structural Genomics target ER541-37-162

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.
PDB ID: 2K1GDownload
MMDB ID: 63048
PDB Deposition Date: 2008/3/3
Updated in MMDB: 2011/10
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2K1G: monomeric; determined by author
Molecular Components in 2K1G
Label Count Molecule
Protein (1 molecule)
Lipoprotein SPR(Gene symbol: mepS)
Molecule annotation
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