8g52: Difference between revisions

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'''Unreleased structure'''


The entry 8g52 is ON HOLD  until Paper Publication
==Crystal structure of a bacterial TPAT family transporter==
<StructureSection load='8g52' size='340' side='right'caption='[[8g52]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8g52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enhygromyxa_salina Enhygromyxa salina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G52 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=8g52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g52 OCA], [https://pdbe.org/8g52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g52 RCSB], [https://www.ebi.ac.uk/pdbsum/8g52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g52 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0C2DGE5_9DELT A0A0C2DGE5_9DELT]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial acquisition of metabolites is largely facilitated by transporters with unique substrate scopes. The tripartite ATP-independent periplasmic (TRAP) transporters comprise a large family of bacterial proteins that facilitate the uptake of a variety of small molecules. It has been reported that some TRAP systems encode a fourth protein, the T component. The T-component, or TatT, is predicted to be a periplasmic-facing lipoprotein that enables the uptake of metabolites from the outer membrane. However, no substrates were revealed for any TatT and their functional role(s) remained enigmatic. We recently identified a homolog in Methylococcus capsulatus that binds to sterols, and herein, we report two additional homologs that demonstrate a preference for long-chain fatty acids. Our bioinformatics, quantitative analyses of protein-ligand interactions, and high-resolution crystal structures suggest that TatTs might facilitate the trafficking of hydrophobic or lipophilic substrates and represent a new class of bacterial lipid and fatty acid transporters.


Authors: Dassama, L.M.K., Zhai, L.
Structures and mechanisms of a novel bacterial transport system for fatty acids.,Zhai L, Chou JC, Oo H, Dassama L Chembiochem. 2023 May 12:e202300156. doi: 10.1002/cbic.202300156. PMID:37170829<ref>PMID:37170829</ref>


Description: Crystal structure of a bacterial TPAT family transporter
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Zhai, L]]
<div class="pdbe-citations 8g52" style="background-color:#fffaf0;"></div>
[[Category: Dassama, L.M.K]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enhygromyxa salina]]
[[Category: Large Structures]]
[[Category: Dassama LMK]]
[[Category: Zhai L]]
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