View source for 4ain


==Crystal structure of BetP with asymmetric protomers.==
<StructureSection load='4ain' size='340' side='right'caption='[[4ain]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ain]] 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=4AIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AIN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BET:TRIMETHYL+GLYCINE'>BET</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CM5:5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE'>CM5</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4ain FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ain OCA], [https://pdbe.org/4ain PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ain RCSB], [https://www.ebi.ac.uk/pdbsum/4ain PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ain ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL] High-affinity uptake of glycine betaine (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Betaine and Na(+) symport has been extensively studied in the osmotically regulated transporter BetP from Corynebacterium glutamicum, a member of the betaine/choline/carnitine transporter family, which shares the conserved LeuT-like fold of two inverted structural repeats. BetP adjusts its transport activity by sensing the cytoplasmic K(+) concentration as a measure for hyperosmotic stress via the osmosensing carboxy-terminal domain. BetP needs to be in a trimeric state for communication between individual protomers through several intratrimeric interaction sites. Recently, crystal structures of inward-facing BetP trimers have contributed to our understanding of activity regulation on a molecular level. Here we report new crystal structures, which reveal two conformationally asymmetric BetP trimers, capturing among them three distinct transport states. We observe a total of four new conformations at once: an outward-open apo and an outward-occluded apo state, and two closed transition states-one in complex with betaine and one substrate-free. On the basis of these new structures, we identified local and global conformational changes in BetP that underlie the molecular transport mechanism, which partially resemble structural changes observed in other sodium-coupled LeuT-like fold transporters, but show differences we attribute to the osmolytic nature of betaine, the exclusive substrate specificity and the regulatory properties of BetP.

Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP.,Perez C, Koshy C, Yildiz O, Ziegler C Nature. 2012 Sep 2. doi: 10.1038/nature11403. PMID:22940865<ref>PMID:22940865</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ain" style="background-color:#fffaf0;"></div>

==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Corynebacterium glutamicum]]
[[Category: Large Structures]]
[[Category: Koshy C]]
[[Category: Yildiz O]]
[[Category: Ziegler C]]