2mhk: Difference between revisions
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mhk RCSB], [http://www.ebi.ac.uk/pdbsum/2mhk PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mhk RCSB], [http://www.ebi.ac.uk/pdbsum/2mhk PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The bacterial cell envelope contains the stress-bearing peptidoglycan layer, which is enlarged during cell growth and division by membrane-anchored synthases guided by cytoskeletal elements. In Escherichia coli, the major peptidoglycan synthase PBP1A requires stimulation by the outer-membrane-anchored lipoprotein LpoA. Whereas the C-terminal domain of LpoA interacts with PBP1A to stimulate its peptide crosslinking activity, little is known about the role of the N-terminal domain. Herein we report its NMR structure, which adopts an all-alpha-helical fold comprising a series of helix-turn-helix tetratricopeptide-repeat (TPR)-like motifs. NMR spectroscopy of full-length LpoA revealed two extended flexible regions in the C-terminal domain and limited, if any, flexibility between the N- and C-terminal domains. Analytical ultracentrifugation and small-angle X-ray scattering results are consistent with LpoA adopting an elongated shape, with dimensions sufficient to span from the outer membrane through the periplasm to interact with the peptidoglycan synthase PBP1A. | |||
Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation.,Jean NL, Bougault CM, Lodge A, Derouaux A, Callens G, Egan AJ, Ayala I, Lewis RJ, Vollmer W, Simorre JP Structure. 2014 Jul 8;22(7):1047-54. doi: 10.1016/j.str.2014.04.017. Epub 2014, Jun 19. PMID:24954617<ref>PMID:24954617</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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