3b5z: Difference between revisions

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{{Seed}}
[[Image:3b5z.png|left|200px]]


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==Crystal Structure of MsbA from Salmonella typhimurium with ADP Vanadate==
The line below this paragraph, containing "STRUCTURE_3b5z", creates the "Structure Box" on the page.
<StructureSection load='3b5z' size='340' side='right'caption='[[3b5z]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
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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]] 4.2&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
{{STRUCTURE_3b5z|  PDB=3b5z  |  SCENE= }}
<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.


===Crystal Structure of MsbA from Salmonella typhimurium with ADP Vanadate===
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>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3b5z" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 18024585 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18024585}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3B5Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B5Z OCA].
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
 
[[Category: Chang G]]
==Reference==
[[Category: Reyes CL]]
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://www.ncbi.nlm.nih.gov/pubmed/18024585 18024585]
[[Category: Roth CB]]
[[Category: Salmonella typhimurium]]
[[Category: Ward A]]
[[Category: Single protein]]
[[Category: Yu J]]
[[Category: Chang, G.]]
[[Category: Reyes, C L.]]
[[Category: Roth, C B.]]
[[Category: Ward, A.]]
[[Category: Yu, J.]]
[[Category: Abc transporter]]
[[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/3b5z"