3b5x: Difference between revisions

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New page: left|200px<br /><applet load="3b5x" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b5x, resolution 5.500Å" /> '''Crystal Structure o...
 
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[[Image:3b5x.jpg|left|200px]]<br /><applet load="3b5x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3b5x, resolution 5.500&Aring;" />
'''Crystal Structure of MsbA from Vibrio cholerae'''<br />


==Overview==
==Crystal Structure of MsbA from Vibrio cholerae==
ATP-binding cassette (ABC) transporters are integral membrane proteins, that translocate a wide variety of substrates across cellular membranes, and are conserved from bacteria to humans. Here we compare four x-ray, structures of the bacterial ABC lipid flippase, MsbA, trapped in different, conformations, two nucleotide-bound structures and two in the absence of, nucleotide. Comparison of the nucleotide-free conformations of MsbA, reveals a flexible hinge formed by extracellular loops 2 and 3. This hinge, allows the nucleotide-binding domains to disassociate while the, ATP-binding half sites remain facing each other. The binding of the, nucleotide causes a packing rearrangement of the transmembrane helices and, changes the accessibility of the transporter from cytoplasmic (inward), facing to extracellular (outward) facing. The inward and outward openings, are mediated by two different sets of transmembrane helix interactions., Altogether, the conformational changes between these structures suggest, that large ranges of motion may be required for substrate transport.
<StructureSection load='3b5x' size='340' side='right'caption='[[3b5x]], [[Resolution|resolution]] 5.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[3b5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B5X FirstGlance]. <br>
3B5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B5X OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5.5&#8491;</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=3b5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5x OCA], [https://pdbe.org/3b5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b5x RCSB], [https://www.ebi.ac.uk/pdbsum/3b5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b5x ProSAT]</span></td></tr>
==Reference==
</table>
Flexibility in the ABC transporter MsbA: Alternating access with a twist., Ward A, Reyes CL, Yu J, Roth CB, Chang G, Proc Natl Acad Sci U S A. 2007 Nov 27;104(48):19005-10. Epub 2007 Nov 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18024585 18024585]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/MSBA_VIBCH MSBA_VIBCH] Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/3b5x_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3b5x ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Vibrio cholerae]]
[[Category: Reyes, C.L.]]
[[Category: Chang G]]
[[Category: Roth, C.B.]]
[[Category: Reyes CL]]
[[Category: Ward, A.]]
[[Category: Roth CB]]
[[Category: Yu, J.]]
[[Category: Ward A]]
[[Category: abc transporter]]
[[Category: Yu J]]
[[Category: atp-binding]]
[[Category: hydrolase]]
[[Category: inner membrane]]
[[Category: lipid flippase]]
[[Category: lipid transport]]
[[Category: membrane]]
[[Category: membrane protein]]
[[Category: msba]]
[[Category: nucleotide-binding]]
[[Category: transmembrane]]
 
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Retrieved from "https://proteopedia.org/3b5x"