Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ King DT, Lameignere E, Strynadka NC. Structural insights into the lipoprotein outer-membrane regulator of penicillin-binding protein 1B. J Biol Chem. 2014 May 7. pii: jbc.M114.565879. PMID:24808177 doi:http://dx.doi.org/10.1074/jbc.M114.565879