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| | <StructureSection load='6lh0' size='340' side='right'caption='[[6lh0]], [[Resolution|resolution]] 2.81Å' scene=''> | | <StructureSection load='6lh0' size='340' side='right'caption='[[6lh0]], [[Resolution|resolution]] 2.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6lh0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33641 Atcc 33641]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LH0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LH0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6lh0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_frederiksenii Yersinia frederiksenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LH0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A6L:2,3-dihydroxypropyl+(9Z)-octadec-9-enoate'>A6L</scene></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]] 2.812Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6lgv|6lgv]], [[6lgy|6lgy]], [[6lgz|6lgz]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A6L:2,3-dihydroxypropyl+(9Z)-octadec-9-enoate'>A6L</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NCTC11470_02445 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29484 ATCC 33641])</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=6lh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lh0 OCA], [https://pdbe.org/6lh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lh0 RCSB], [https://www.ebi.ac.uk/pdbsum/6lh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lh0 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=6lh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lh0 OCA], [http://pdbe.org/6lh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lh0 RCSB], [http://www.ebi.ac.uk/pdbsum/6lh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lh0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A380PV03_YERFR A0A380PV03_YERFR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33641]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ji, Y]] | + | [[Category: Yersinia frederiksenii]] |
| - | [[Category: Lyu, Y]] | + | [[Category: Ji Y]] |
| - | [[Category: Sun, Z]] | + | [[Category: Lyu Y]] |
| - | [[Category: Wang, X]] | + | [[Category: Sun Z]] |
| - | [[Category: Zhou, X]] | + | [[Category: Wang X]] |
| - | [[Category: Asbt]]
| + | [[Category: Zhou X]] |
| - | [[Category: Bile acid transporter]]
| + | |
| - | [[Category: Ntcp]]
| + | |
| - | [[Category: Slc10]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
A0A380PV03_YERFR
Publication Abstract from PubMed
Apical sodium-dependent bile acid transporter (ASBT) retrieves bile acids from the small intestine and plays a pivotal role in enterohepatic circulation. Currently, high-resolution structures are available for two bacterial ASBT homologs (ASBTNM from Neisseria meningitides and ASBTYf from Yersinia frederiksenii), from which an elevator-style alternating-access mechanism has been proposed for substrate transport. A key concept in this model is that the substrate binds to the central cavity of the transporter so that the elevator-like motion can expose the bound substrate alternatingly to either side of the membrane during a transport cycle. However, no structure of an ASBT has been solved with a substrate bound in its central cavity, so how a substrate binds to ASBT remains to be defined. In this study, molecular docking, structure determination and functional analysis were combined to define and validate the details of substrate binding in ASBTYf. The findings provide coherent evidence to provide a clearer picture of how the substrate binds in the central cavity of ASBTYf that fits the alternating-access model.
Substrate binding in the bile acid transporter ASBTYf from Yersinia frederiksenii.,Wang X, Lyu Y, Ji Y, Sun Z, Zhou X Acta Crystallogr D Struct Biol. 2021 Jan 1;77(Pt 1):117-125. doi:, 10.1107/S2059798320015004. Epub 2021 Jan 1. PMID:33404531[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang X, Lyu Y, Ji Y, Sun Z, Zhou X. Substrate binding in the bile acid transporter ASBTYf from Yersinia frederiksenii. Acta Crystallogr D Struct Biol. 2021 Jan 1;77(Pt 1):117-125. doi:, 10.1107/S2059798320015004. Epub 2021 Jan 1. PMID:33404531 doi:http://dx.doi.org/10.1107/S2059798320015004
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