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| | <SX load='6o84' size='340' side='right' viewer='molstar' caption='[[6o84]], [[Resolution|resolution]] 3.92Å' scene=''> | | <SX load='6o84' size='340' side='right' viewer='molstar' caption='[[6o84]], [[Resolution|resolution]] 3.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o84]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Silurana_(xenopus)_tropicalis Silurana (xenopus) tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O84 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6O84 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o84]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O84 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.92Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">otop3, LOC100127796 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8364 Silurana (Xenopus) tropicalis])</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=6o84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o84 OCA], [https://pdbe.org/6o84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o84 RCSB], [https://www.ebi.ac.uk/pdbsum/6o84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o84 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6o84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o84 OCA], [http://pdbe.org/6o84 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o84 RCSB], [http://www.ebi.ac.uk/pdbsum/6o84 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o84 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OTOP3_XENTR OTOP3_XENTR] Proton-selective channel gated by extracellular protons.<ref>PMID:30973323</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bai, X C]] | + | [[Category: Xenopus tropicalis]] |
| - | [[Category: Chen, Q F]] | + | [[Category: Bai XC]] |
| - | [[Category: Jiang, Y X]] | + | [[Category: Chen QF]] |
| - | [[Category: Channel]] | + | [[Category: Jiang YX]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Otopetrin]]
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| - | [[Category: Proton]]
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| Structural highlights
Function
OTOP3_XENTR Proton-selective channel gated by extracellular protons.[1]
Publication Abstract from PubMed
The otopetrin (OTOP) proteins were recently characterized as proton channels. Here we present the cryo-EM structure of OTOP3 from Xenopus tropicalis (XtOTOP3) along with functional characterization of the channel. XtOTOP3 forms a homodimer with each subunit containing 12 transmembrane helices that can be divided into two structurally homologous halves; each half assembles as an alpha-helical barrel that could potentially serve as a proton conduction pore. Both pores open from the extracellular half before becoming occluded at a central constriction point consisting of three highly conserved residues - Gln232/585-Asp262/Asn623-Tyr322/666 (the constriction triads). Mutagenesis shows that the constriction triad from the second pore is less amenable to perturbation than that of the first pore, suggesting an unequal contribution between the two pores to proton transport. We also identified several key residues at the interface between the two pores that are functionally important, particularly Asp509, which confers intracellular pH-dependent desensitization to OTOP channels.
Structural and functional characterization of an otopetrin family proton channel.,Chen Q, Zeng W, She J, Bai X, Jiang Y Elife. 2019 Apr 11;8. pii: 46710. doi: 10.7554/eLife.46710. PMID:30973323[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen Q, Zeng W, She J, Bai X, Jiang Y. Structural and functional characterization of an otopetrin family proton channel. Elife. 2019 Apr 11;8. pii: 46710. doi: 10.7554/eLife.46710. PMID:30973323 doi:http://dx.doi.org/10.7554/eLife.46710
- ↑ Chen Q, Zeng W, She J, Bai X, Jiang Y. Structural and functional characterization of an otopetrin family proton channel. Elife. 2019 Apr 11;8. pii: 46710. doi: 10.7554/eLife.46710. PMID:30973323 doi:http://dx.doi.org/10.7554/eLife.46710
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