6f2w
From Proteopedia
(Difference between revisions)
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<StructureSection load='6f2w' size='340' side='right'caption='[[6f2w]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='6f2w' size='340' side='right'caption='[[6f2w]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6f2w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6f2w]] 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=6F2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2W FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f2g|6f2g]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f2g|6f2g]]</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='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=6f2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2w OCA], [http://pdbe.org/6f2w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2w RCSB], [http://www.ebi.ac.uk/pdbsum/6f2w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2w ProSAT]</span></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=6f2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2w OCA], [http://pdbe.org/6f2w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2w RCSB], [http://www.ebi.ac.uk/pdbsum/6f2w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:31000719</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6f2w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Camelus glama]] | ||
| + | [[Category: Carnobacterium sp. at7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Carpena, X]] | [[Category: Carpena, X]] | ||
Current revision
Bacterial asc transporter crystal structure in open to in conformation
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