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New page: left|200px<br /><applet load="3b5z" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b5z, resolution 4.200Å" /> '''Crystal Structure o...
 
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[[Image:3b5z.jpg|left|200px]]<br /><applet load="3b5z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3b5z, resolution 4.200&Aring;" />
'''Crystal Structure of MsbA from Salmonella typhimurium with ADP Vanadate'''<br />


==Overview==
==Crystal Structure of MsbA from Salmonella typhimurium with ADP Vanadate==
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='3b5z' size='340' side='right'caption='[[3b5z]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3b5z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B5Z 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]] 4.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=3b5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5z OCA], [https://pdbe.org/3b5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b5z RCSB], [https://www.ebi.ac.uk/pdbsum/3b5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b5z ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MSBA_SALTY MSBA_SALTY] 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/b5/3b5z_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3b5z ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==About this Structure==
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:18024585<ref>PMID:18024585</ref>
3B5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B5Z OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Salmonella typhimurium]]
<div class="pdbe-citations 3b5z" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Reyes, C.L.]]
<references/>
[[Category: Roth, C.B.]]
__TOC__
[[Category: Ward, A.]]
</StructureSection>
[[Category: Yu, J.]]
[[Category: Large Structures]]
[[Category: ADP]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: abc transporter]]
[[Category: Chang G]]
[[Category: atp-binding]]
[[Category: Reyes CL]]
[[Category: hydrolase]]
[[Category: Roth CB]]
[[Category: inner membrane]]
[[Category: Ward A]]
[[Category: lipid flippase]]
[[Category: Yu J]]
[[Category: lipid transport]]
[[Category: membrane]]
[[Category: membrane protein]]
[[Category: msba]]
[[Category: nucleotide-binding]]
[[Category: transmembrane]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:54:38 2008''

Latest revision as of 08:56, 13 August 2026

Crystal Structure of MsbA from Salmonella typhimurium with ADP Vanadate

3b5z, resolution 4.20Å

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