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 [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4DBL 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]] 3.493Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4dbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbl OCA], [https://pdbe.org/4dbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dbl RCSB], [https://www.ebi.ac.uk/pdbsum/4dbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BTUC_ECOLI BTUC_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.[HAMAP-Rule:MF_01004] | |||
<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> | |||
<div class="pdbe-citations 4dbl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Hvorup RN]] | |||
[[Category: Korkhov VM]] | |||
[[Category: Locher KP]] | |||
[[Category: Mireku SM]] | |||
Latest revision as of 09:55, 30 October 2024
Crystal structure of E159Q mutant of BtuCDF
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