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| | <StructureSection load='6f2g' size='340' side='right'caption='[[6f2g]], [[Resolution|resolution]] 2.92Å' scene=''> | | <StructureSection load='6f2g' size='340' side='right'caption='[[6f2g]], [[Resolution|resolution]] 2.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6f2g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama] and [http://en.wikipedia.org/wiki/Carnobacterium_sp._at7 Carnobacterium sp. at7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6f2g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Carnobacterium_sp._AT7 Carnobacterium sp. AT7] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F2G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.92Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAT7_03719 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=333990 Carnobacterium sp. AT7])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2g OCA], [http://pdbe.org/6f2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2g RCSB], [http://www.ebi.ac.uk/pdbsum/6f2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2g ProSAT]</span></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=6f2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2g OCA], [https://pdbe.org/6f2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f2g RCSB], [https://www.ebi.ac.uk/pdbsum/6f2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6f2g" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6f2g" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Antibody 3D structures|Antibody 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Camelus glama]] | + | [[Category: Carnobacterium sp. AT7]] |
| - | [[Category: Carnobacterium sp. at7]] | + | [[Category: Lama glama]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carpena, X]] | + | [[Category: Carpena X]] |
| - | [[Category: Errasti-Murugarren, E]] | + | [[Category: Errasti-Murugarren E]] |
| - | [[Category: Fita, I]] | + | [[Category: Fita I]] |
| - | [[Category: Fort, J]] | + | [[Category: Fort J]] |
| - | [[Category: Palacin, M]] | + | [[Category: Palacin M]] |
| - | [[Category: Apc transporter]]
| + | |
| - | [[Category: Lat transporter]]
| + | |
| - | [[Category: Leut fold]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Publication Abstract from PubMed
L-amino acid transporters (LATs) play key roles in human physiology and are implicated in several human pathologies. LATs are asymmetric amino acid exchangers where the low apparent affinity cytoplasmic side controls the exchange of substrates with high apparent affinity on the extracellular side. Here, we report the crystal structures of an LAT, the bacterial alanine-serine-cysteine exchanger (BasC), in a non-occluded inward-facing conformation in both apo and substrate-bound states. We crystallized BasC in complex with a nanobody, which blocks the transporter from the intracellular side, thus unveiling the sidedness of the substrate interaction of BasC. Two conserved residues in human LATs, Tyr 236 and Lys 154, are located in equivalent positions to the Na1 and Na2 sites of sodium-dependent APC superfamily transporters. Functional studies and molecular dynamics (MD) calculations reveal that these residues are key for the asymmetric substrate interaction of BasC and in the homologous human transporter Asc-1.
L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction.,Errasti-Murugarren E, Fort J, Bartoccioni P, Diaz L, Pardon E, Carpena X, Espino-Guarch M, Zorzano A, Ziegler C, Steyaert J, Fernandez-Recio J, Fita I, Palacin M Nat Commun. 2019 Apr 18;10(1):1807. doi: 10.1038/s41467-019-09837-z. PMID:31000719[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Errasti-Murugarren E, Fort J, Bartoccioni P, Diaz L, Pardon E, Carpena X, Espino-Guarch M, Zorzano A, Ziegler C, Steyaert J, Fernandez-Recio J, Fita I, Palacin M. L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction. Nat Commun. 2019 Apr 18;10(1):1807. doi: 10.1038/s41467-019-09837-z. PMID:31000719 doi:http://dx.doi.org/10.1038/s41467-019-09837-z
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