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3p03

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==Crystal structure of BetP-G153D with choline bound==
==Crystal structure of BetP-G153D with choline bound==
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<StructureSection load='3p03' size='340' side='right' caption='[[3p03]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
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<StructureSection load='3p03' size='340' side='right'caption='[[3p03]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p03]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P03 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p03]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P03 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">betP, Cgl0892, cg1016 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene></td></tr>
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<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=3p03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p03 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p03 RCSB], [http://www.ebi.ac.uk/pdbsum/3p03 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p03 OCA], [https://pdbe.org/3p03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p03 RCSB], [https://www.ebi.ac.uk/pdbsum/3p03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p03 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL]] High-affinity uptake of glycine betaine (By similarity).
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[https://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL] High-affinity uptake of glycine betaine (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BetP is an Na(+)-coupled betaine-specific transporter of the betaine-choline-carnitine (BCC) transporter family involved in the response to hyperosmotic stress. The crystal structure of BetP revealed an overall fold of two inverted structurally related repeats (LeuT-fold) that BetP shares with other sequence-unrelated Na(+)-coupled symporters. Numerous structures of LeuT-fold transporters in distinct conformational states have contributed substantially to our understanding of the alternating access mechanism of transport. Nevertheless, coupling of substrate and co-transported ion fluxes has not been structurally corroborated to the same extent. We converted BetP by a single-point mutation-glycine to aspartate-into an H(+)-coupled choline-specific transporter and solved the crystal structure of this mutant in complex with choline. The structure of BetP-G153D demonstrates a new inward-facing open conformation for BetP. Choline binding to a location close to the second, low-affinity sodium-binding site (Na2) of LeuT-fold transporters is facilitated by the introduced aspartate. Our data confirm the importance of a cation-binding site in BetP, playing a key role in a proposed molecular mechanism of Na(+) and H(+) coupling in BCC transporters.
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Substrate specificity and ion coupling in the Na(+)/betaine symporter BetP.,Perez C, Koshy C, Ressl S, Nicklisch S, Kramer R, Ziegler C EMBO J. 2011 Mar 1. PMID:21364531<ref>PMID:21364531</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Symporter 3D structures|Symporter 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
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[[Category: Perez, C]]
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[[Category: Large Structures]]
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[[Category: Ressl, S]]
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[[Category: Perez C]]
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[[Category: Ziegler, Z]]
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[[Category: Ressl S]]
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[[Category: Secondary transporter]]
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[[Category: Ziegler Z]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of BetP-G153D with choline bound

PDB ID 3p03

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