3hfx
From Proteopedia
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<StructureSection load='3hfx' size='340' side='right'caption='[[3hfx]], [[Resolution|resolution]] 3.15Å' scene=''> | <StructureSection load='3hfx' size='340' side='right'caption='[[3hfx]], [[Resolution|resolution]] 3.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hfx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3hfx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFX FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=3hfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfx OCA], [https://pdbe.org/3hfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfx RCSB], [https://www.ebi.ac.uk/pdbsum/3hfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfx 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=3hfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfx OCA], [https://pdbe.org/3hfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfx RCSB], [https://www.ebi.ac.uk/pdbsum/3hfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/CAIT_ECOLI CAIT_ECOLI] Catalyzes the exchange of L-carnitine for gamma-butyrobetaine and related betaines. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hfx ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hfx ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | CaiT is a membrane antiporter that catalyzes the exchange of L-carnitine with gamma-butyrobetaine across the Escherichia coli membrane. To obtain structural insights into the antiport mechanism, we solved the crystal structure of CaiT at a resolution of 3.15 A. We crystallized CaiT as a homotrimer complex, in which each protomer contained 12 transmembrane helices and 4 l-carnitine molecules outlining the transport pathway across the membrane. Mutagenesis studies revealed a primary binding site at the center of the protein and a secondary substrate-binding site at the bottom of the intracellular vestibule. These results, together with the insights obtained from structural comparison with structurally homologous transporters, provide mechanistic insights into the association between substrate translocation and the conformational changes of CaiT. | ||
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| - | Crystal structure of the carnitine transporter and insights into the antiport mechanism.,Tang L, Bai L, Wang WH, Jiang T Nat Struct Mol Biol. 2010 Apr;17(4):492-6. Epub 2010 Mar 28. PMID:20357772<ref>PMID:20357772</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3hfx" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bai | + | [[Category: Bai L]] |
| - | [[Category: Jiang | + | [[Category: Jiang T]] |
| - | [[Category: Tang | + | [[Category: Tang L]] |
| - | [[Category: Wang | + | [[Category: Wang W-H]] |
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Current revision
Crystal structure of carnitine transporter
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