2K1G

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

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2K1G の概要

• エントリーDOI: 10.2210/pdb2k1g/pdb
• NMR情報: BMRB: 15603
• 分子名称: Lipoprotein spr (1 entity in total)
• 機能のキーワード: 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
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell membrane; Lipid-anchor (Potential): P0AFV4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15584.57

構造登録者

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) (登録日: 2008-03-03, 公開日: 2008-03-18, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

SOLUTION NMR