4Q6Z

LpoB C-terminal domain from Escherichia coli

Summary for 4Q6Z

• Entry DOI: 10.2210/pdb4q6z/pdb
• Related: 4Q6L 4Q6V
• Descriptor: Penicillin-binding protein activator LpoB (2 entities in total)
• Functional Keywords: mixed alpha-beta, lipoprotein, activator of pbp1b, pbp1b, lipidation, outer-membrane, protein binding
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Lipid-anchor; Periplasmic side (By similarity): Q1RD49
• Total number of polymer chains: 2
• Total formula weight: 28470.07

Authors

King, D.T.,Strynadka, N.C.J. (deposition date: 2014-04-23, release date: 2014-05-14, Last modification date: 2024-02-28)

Primary citation

King, D.T.,Lameignere, E.,Strynadka, N.C.
Structural Insights into the Lipoprotein Outer Membrane Regulator of Penicillin-binding Protein 1B.
J.Biol.Chem., 289:19245-19253, 2014

PubMed Abstract: 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.

PubMed: 24808177
DOI: 10.1074/jbc.M114.565879

Experimental method

X-RAY DIFFRACTION (2.8 Å)