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8g53
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a bacterial TPAT family transporter== | |
| + | <StructureSection load='8g53' size='340' side='right'caption='[[8g53]], [[Resolution|resolution]] 1.03Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8g53]] is a 1 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=8G53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G53 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=8g53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g53 OCA], [https://pdbe.org/8g53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g53 RCSB], [https://www.ebi.ac.uk/pdbsum/8g53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g53 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0C1ZR44_9DELT A0A0C1ZR44_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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8g53" style="background-color:#fffaf0;"></div> |
| - | [[Category: Dassama | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Enhygromyxa salina]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dassama LMK]] | ||
| + | [[Category: Zhai L]] | ||
Revision as of 04:06, 25 May 2023
Crystal structure of a bacterial TPAT family transporter
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