4doj

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4doj]] 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=4DOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DOJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4doj]] 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=4DOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DOJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PGT:(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PGT</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]] 3.25&#8491;</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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PGT:(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PGT</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=4doj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4doj OCA], [https://pdbe.org/4doj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4doj RCSB], [https://www.ebi.ac.uk/pdbsum/4doj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4doj 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=4doj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4doj OCA], [https://pdbe.org/4doj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4doj RCSB], [https://www.ebi.ac.uk/pdbsum/4doj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4doj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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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[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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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4doj" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
*[[Symporter 3D structures|Symporter 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of BetP in outward-facing conformation

PDB ID 4doj

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