3p03: Difference between revisions
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==Crystal structure of BetP-G153D with choline bound== | |||
=== | <StructureSection load='3p03' size='340' side='right' caption='[[3p03]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</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> | |||
<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> | |||
<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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Corynebacterium glutamicum]] | [[Category: Corynebacterium glutamicum]] | ||
[[Category: Perez, C | [[Category: Perez, C]] | ||
[[Category: Ressl, S | [[Category: Ressl, S]] | ||
[[Category: Ziegler, Z | [[Category: Ziegler, Z]] | ||
[[Category: Secondary transporter]] | [[Category: Secondary transporter]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 09:35, 19 December 2014
Crystal structure of BetP-G153D with choline boundCrystal structure of BetP-G153D with choline bound
Structural highlights
Publication Abstract from PubMedBetP 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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