8g53
From Proteopedia
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== Structural highlights == | == 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> | <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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.03Å</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> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/A0A0C1ZR44_9BACT A0A0C1ZR44_9BACT] |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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 | + | Structures and Mechanisms of a Novel Bacterial Transport System for Fatty Acids.,Zhai L, Chou JC, Oo H, Dassama LMK Chembiochem. 2023 Aug 1;24(15):e202300156. doi: 10.1002/cbic.202300156. Epub 2023 , Jul 6. PMID:37170829<ref>PMID:37170829</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Crystal structure of a bacterial TPAT family transporter
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