3p03: Difference between revisions
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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> | <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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== Function == | |||
[[http://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL]] High-affinity uptake of glycine betaine (By similarity). | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 08:19, 25 December 2014
Crystal structure of BetP-G153D with choline boundCrystal structure of BetP-G153D with choline bound
Structural highlights
Function[BETP_CORGL] High-affinity uptake of glycine betaine (By similarity). 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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