2K1G

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

Replaces:  2JYX

Summary for 2K1G

• Entry DOI: 10.2210/pdb2k1g/pdb
• NMR Information: BMRB: 15603
• Descriptor: Lipoprotein spr (1 entity in total)
• Functional Keywords: solution nmr structure, bacterial lipoprotein, cysteine peptidase, nplc/p60 family, construct optimized, membrane, palmitate, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, lipoprotein
• Biological source: Escherichia coli
• Cellular location: Cell membrane; Lipid-anchor (Potential): P0AFV4
• Total number of polymer chains: 1
• Total formula weight: 15584.57

Authors

Aramini, J.M.,Rossi, P.,Zhao, L.,Jiang, M.,Maglaqui, M.,Xiao, R.,Liu, J.,Baran, M.C.,Swapna, G.V.T.,Huang, Y.J.,Acton, T.B.,Rost, B.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2008-03-03, release date: 2008-03-18, Last modification date: 2024-05-01)

Primary citation

Aramini, J.M.,Rossi, P.,Huang, Y.J.,Zhao, L.,Jiang, M.,Maglaqui, M.,Xiao, R.,Locke, J.,Nair, R.,Rost, B.,Acton, T.B.,Inouye, M.,Montelione, G.T.
Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad.
Biochemistry, 47:9715-9717, 2008

PubMed 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 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.

PubMed: 18715016
DOI: 10.1021/bi8010779

Experimental method

SOLUTION NMR