4q6v

LpoB C-terminal domain from Salmonella enterica (Sel-Met)

spinqualitylabelsall models 4q6v, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q6v is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.97Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LPOB_SALTY Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b) (By similarity). Publication Abstract from PubMed In bacteria, the synthesis of the protective peptidoglycan sacculus is a dynamic process that is tightly regulated at multiple levels. Recently, the lipoprotein co-factor LpoB has been found essential for the in-vivo function of the major peptidoglycan synthase PBP1b in Enterobacteriaceae. Herein, we reveal the crystal structures of Salmonella enterica and Escherichia coli LpoB. The LpoB protein can be modeled as a ball and tether, consisting of a disordered N-terminal region, followed by a compact globular C-terminal domain. Taken together, our structural data allows us to propose a revised model for LpoB mediated regulation of peptidoglycan synthesis. Structural insights into the lipoprotein outer-membrane regulator of penicillin-binding protein 1B.,King DT, Lameignere E, Strynadka NC J Biol Chem. 2014 May 7. pii: jbc.M114.565879. PMID:24808177 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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