4q6z
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4q6z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q6Z FirstGlance]. <br> | <table><tr><td colspan='2'>[[4q6z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q6Z FirstGlance]. <br> | ||
| - | </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=4q6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q6z OCA], [https://pdbe.org/4q6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q6z RCSB], [https://www.ebi.ac.uk/pdbsum/4q6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q6z ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=4q6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q6z OCA], [https://pdbe.org/4q6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q6z RCSB], [https://www.ebi.ac.uk/pdbsum/4q6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q6z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q1RD49_ECOUT Q1RD49_ECOUT] Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b) (By similarity).[HAMAP-Rule:MF_01889] | [https://www.uniprot.org/uniprot/Q1RD49_ECOUT Q1RD49_ECOUT] Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b) (By similarity).[HAMAP-Rule:MF_01889] | ||
| - | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4q6z" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
LpoB C-terminal domain from Escherichia coli
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