4Q6V
LpoB C-terminal domain from Salmonella enterica (Sel-Met)
Summary for 4Q6V
| Entry DOI | 10.2210/pdb4q6v/pdb |
| Related | 4Q6L 4Q6Z |
| 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 | Salmonella enterica subsp. enterica serovar Typhimurium |
| Cellular location | Cell outer membrane; Lipid-anchor; Periplasmic side (By similarity): Q8ZQ08 |
| Total number of polymer chains | 1 |
| Total formula weight | 14594.64 |
| Authors | King, D.T.,Strynadka, N.C.J. (deposition date: 2014-04-23, release date: 2014-05-14, Last modification date: 2024-11-06) |
| 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 Cited by 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: 24808177DOI: 10.1074/jbc.M114.565879 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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