4q6v: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: '''Unreleased structure''' The entry 4q6v is ON HOLD Authors: King, D.T., Strynadka, N.C.J. Description: LpoB C-terminal domain from Salmonella enterica (Sel-Met)
 
OCA (talk | contribs)
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4q6v is ON HOLD
==LpoB C-terminal domain from Salmonella enterica (Sel-Met)==
<StructureSection load='4q6v' size='340' side='right'caption='[[4q6v]], [[Resolution|resolution]] 1.97&Aring;' 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]] 1.97&#8491;</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.


Authors: King, D.T., Strynadka, N.C.J.
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>


Description: LpoB C-terminal domain from Salmonella enterica (Sel-Met)
From MEDLINE&reg;/PubMed&reg;, 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]]

Latest revision as of 11:18, 6 November 2024

LpoB C-terminal domain from Salmonella enterica (Sel-Met)

4q6v, resolution 1.97Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA