8hpj
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8hpj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HPJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hpj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HPJ 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=8hpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hpj OCA], [https://pdbe.org/8hpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hpj RCSB], [https://www.ebi.ac.uk/pdbsum/8hpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hpj 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]] 3.3Å</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=8hpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hpj OCA], [https://pdbe.org/8hpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hpj RCSB], [https://www.ebi.ac.uk/pdbsum/8hpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hpj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/OXLT_OXAFO OXLT_OXAFO] Anion transporter that carries out the exchange of divalent oxalate with monovalent formate, the product of oxalate decarboxylation, at the plasma membrane, and in doing so catalyzes the vectorial portion of a proton-motive metabolic cycle that drives ATP synthesis.<ref>PMID:8636101</ref> | [https://www.uniprot.org/uniprot/OXLT_OXAFO OXLT_OXAFO] Anion transporter that carries out the exchange of divalent oxalate with monovalent formate, the product of oxalate decarboxylation, at the plasma membrane, and in doing so catalyzes the vectorial portion of a proton-motive metabolic cycle that drives ATP synthesis.<ref>PMID:8636101</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | An oxalate-degrading bacterium in the gut microbiota absorbs food-derived oxalate to use this as a carbon and energy source, thereby reducing the risk of kidney stone formation in host animals. The bacterial oxalate transporter OxlT selectively uptakes oxalate from the gut to bacterial cells with a strict discrimination from other nutrient carboxylates. Here, we present crystal structures of oxalate-bound and ligand-free OxlT in two distinct conformations, occluded and outward-facing states. The ligand-binding pocket contains basic residues that form salt bridges with oxalate while preventing the conformational switch to the occluded state without an acidic substrate. The occluded pocket can accommodate oxalate but not larger dicarboxylates, such as metabolic intermediates. The permeation pathways from the pocket are completely blocked by extensive interdomain interactions, which can be opened solely by a flip of a single side chain neighbouring the substrate. This study shows the structural basis underlying metabolic interactions enabling favourable symbiosis. | ||
| + | |||
| + | Structure and mechanism of oxalate transporter OxlT in an oxalate-degrading bacterium in the gut microbiota.,Jaunet-Lahary T, Shimamura T, Hayashi M, Nomura N, Hirasawa K, Shimizu T, Yamashita M, Tsutsumi N, Suehiro Y, Kojima K, Sudo Y, Tamura T, Iwanari H, Hamakubo T, Iwata S, Okazaki KI, Hirai T, Yamashita A Nat Commun. 2023 Apr 3;14(1):1730. doi: 10.1038/s41467-023-36883-5. PMID:37012268<ref>PMID:37012268</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8hpj" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of the bacterial oxalate transporter OxlT in a ligand-free outward-facing form
| |||||||||||
