4dbl: Difference between revisions
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[[ | ==Crystal structure of E159Q mutant of BtuCDF== | ||
<StructureSection load='4dbl' size='340' side='right' caption='[[4dbl]], [[Resolution|resolution]] 3.49Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4dbl]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBL FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vitamin_B12-transporting_ATPase Vitamin B12-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.33 3.6.3.33] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dbl RCSB], [http://www.ebi.ac.uk/pdbsum/4dbl PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BtuCD is an ABC transporter catalyzing the uptake of vitamin B(12) across the Escherichia coli inner membrane. A previously reported X-ray structure of BtuCD in complex with the periplasmic vitamin B(12)-binding protein BtuF revealed asymmetry of the transmembrane BtuC subunits. The functional relevance of this asymmetry has remained uncertain. Here we report the X-ray structure of a catalytically impaired BtuCD mutant in complex with BtuF, where the BtuC subunits adopt a distinct asymmetric conformation. The structure suggests that BtuF does not discriminate between, or impose, asymmetric conformations of BtuCD. It also explains the conformational disorder observed in BtuCDF crystals. | |||
Asymmetric states of vitamin B12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF.,Korkhov VM, Mireku SA, Hvorup RN, Locher KP FEBS Lett. 2012 Apr 5;586(7):972-6. Epub 2012 Mar 8. PMID:22569249<ref>PMID:22569249</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Vitamin B12-transporting ATPase]] | [[Category: Vitamin B12-transporting ATPase]] | ||
Revision as of 07:41, 5 June 2014
Crystal structure of E159Q mutant of BtuCDF
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