4Q6V: Lpob C-terminal Domain From Salmonella Enterica (sel-met)

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. Here, 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 allow us to propose new insights into LpoB-mediated regulation of peptidoglycan synthesis.
PDB ID: 4Q6VDownload
MMDB ID: 119497
PDB Deposition Date: 2014/4/23
Updated in MMDB: 2014/07
Experimental Method:
x-ray diffraction
Resolution: 1.97  Å
Source Organism:
Similar Structures:
Biological Unit for 4Q6V: monomeric; determined by author and by software (PISA)
Molecular Components in 4Q6V
Label Count Molecule
Protein (1 molecule)
Penicillin-binding Protein Activator Lpob(Gene symbol: ycfM)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB