4q6v
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==LpoB C-terminal domain from Salmonella enterica (Sel-Met)== | |
| + | <StructureSection load='4q6v' size='340' side='right'caption='[[4q6v]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4q6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q6V FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q6v OCA], [https://pdbe.org/4q6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q6v RCSB], [https://www.ebi.ac.uk/pdbsum/4q6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q6v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LPOB_SALTY LPOB_SALTY] Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b) (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24808177</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4q6v" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
| + | [[Category: King DT]] | ||
| + | [[Category: Strynadka NCJ]] | ||
Current revision
LpoB C-terminal domain from Salmonella enterica (Sel-Met)
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