4beg: Difference between revisions

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New page: '''Unreleased structure''' The entry 4beg is ON HOLD until Paper Publication Authors: Holton, S.J., Williams, M. Description: Structure of Rv2140c, a phosphatidyl-ethanolamine binding ...
 
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'''Unreleased structure'''


The entry 4beg is ON HOLD  until Paper Publication
==Structure of Rv2140c, a phosphatidyl-ethanolamine binding protein from Mycobacterium tuberculosis in complex with sulphate==
<StructureSection load='4beg' size='340' side='right'caption='[[4beg]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4beg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BEG 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]] 1.42&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4beg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4beg OCA], [https://pdbe.org/4beg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4beg RCSB], [https://www.ebi.ac.uk/pdbsum/4beg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4beg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y2140_MYCTU Y2140_MYCTU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rv2140c is one of many conserved Mycobacterium tuberculosis proteins for which no molecular function has been identified. We have determined a high-resolution crystal structure of the Rv2140c gene product, which reveals a dimeric complex that shares strong structural homology with the phosphatidylethanolamine-binding family of proteins. Rv2140c forms low-millimolar interactions with a selection of soluble phosphatidylethanolamine analogs, indicating that it has a role in lipid metabolism. Furthermore, the small molecule locostatin binds to the Rv2140c ligand-binding site and also inhibits the growth of the model organism Mycobacterium smegmatis.


Authors: Holton, S.J., Williams, M.
Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis.,Eulenburg G, Higman VA, Diehl A, Wilmanns M, Holton SJ FEBS Lett. 2013 Jul 29. pii: S0014-5793(13)00567-X. doi:, 10.1016/j.febslet.2013.07.038. PMID:23907008<ref>PMID:23907008</ref>


Description: Structure of Rv2140c, a phosphatidyl-ethanolamine binding protein from Mycobacterium tuberculosis in complex with sulphate
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4beg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Holton SJ]]
[[Category: Williams M]]

Latest revision as of 11:49, 20 December 2023

Structure of Rv2140c, a phosphatidyl-ethanolamine binding protein from Mycobacterium tuberculosis in complex with sulphate

4beg, resolution 1.42Å

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