4q6l
From Proteopedia
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<StructureSection load='4q6l' size='340' side='right' caption='[[4q6l]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4q6l' size='340' side='right' caption='[[4q6l]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4q6l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q6L OCA]. <br> | + | <table><tr><td colspan='2'>[[4q6l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q6L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q6L FirstGlance]. <br> |
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q6v|4q6v]], [[4q6z|4q6z]]</td></tr> | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q6v|4q6v]], [[4q6z|4q6z]]</td></tr> | ||
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=4q6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q6l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q6l RCSB], [http://www.ebi.ac.uk/pdbsum/4q6l 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=4q6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q6l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q6l RCSB], [http://www.ebi.ac.uk/pdbsum/4q6l PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <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> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:17, 2 July 2014
LpoB C-terminal domain from Salmonella enterica (Native)
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