3eya: Difference between revisions

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


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==Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli==
The line below this paragraph, containing "STRUCTURE_3eya", creates the "Structure Box" on the page.
<StructureSection load='3eya' size='340' side='right'caption='[[3eya]], [[Resolution|resolution]] 2.50&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'>[[3eya]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EYA FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
{{STRUCTURE_3eya|  PDB=3eya  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eya OCA], [https://pdbe.org/3eya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eya RCSB], [https://www.ebi.ac.uk/pdbsum/3eya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eya ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POXB_ECOLI POXB_ECOLI]
== 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/ey/3eya_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=3eya ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The thiamin- and flavin-dependent peripheral membrane enzyme pyruvate oxidase from E. coli catalyzes the oxidative decarboxylation of the central metabolite pyruvate to CO(2) and acetate. Concomitant reduction of the enzyme-bound flavin triggers membrane binding of the C terminus and shuttling of 2 electrons to ubiquinone 8, a membrane-bound mobile carrier of the electron transport chain. Binding to the membrane in vivo or limited proteolysis in vitro stimulate the catalytic proficiency by 2 orders of magnitude. The molecular mechanisms by which membrane binding and activation are governed have remained enigmatic. Here, we present the X-ray crystal structures of the full-length enzyme and a proteolytically activated truncation variant lacking the last 23 C-terminal residues inferred as important in membrane binding. In conjunction with spectroscopic results, the structural data pinpoint a conformational rearrangement upon activation that exposes the autoinhibitory C terminus, thereby freeing the active site. In the activated enzyme, Phe-465 swings into the active site and wires both cofactors for efficient electron transfer. The isolated C terminus, which has no intrinsic helix propensity, folds into a helical structure in the presence of micelles.


===Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli===
Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli.,Neumann P, Weidner A, Pech A, Stubbs MT, Tittmann K Proc Natl Acad Sci U S A. 2008 Nov 11;105(45):17390-5. Epub 2008 Nov 6. PMID:18988747<ref>PMID:18988747</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3eya" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18988747}}, adds the Publication Abstract to the page
*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18988747 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18988747}}
__TOC__
 
</StructureSection>
==About this Structure==
3EYA is a 12 chains structure of sequences 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=3EYA OCA].
 
==Reference==
<ref group="xtra">PMID:18988747</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Neumann, P.]]
[[Category: Large Structures]]
[[Category: Pech, A.]]
[[Category: Neumann P]]
[[Category: Stubbs, M T.]]
[[Category: Pech A]]
[[Category: Tittmann, K.]]
[[Category: Stubbs MT]]
[[Category: Weidner, A.]]
[[Category: Tittmann K]]
[[Category: Fad]]
[[Category: Weidner A]]
[[Category: Flavoprotein]]
[[Category: Interactions with lipids cell membrane]]
[[Category: Lipid-binding]]
[[Category: Magnesium]]
[[Category: Membrane]]
[[Category: Membrane-associated flavoprotein dehydrogenase]]
[[Category: Oxidoreductase]]
[[Category: Pyruvate oxidase]]
[[Category: Thiamine pyrophosphate]]
 
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Retrieved from "https://proteopedia.org/3eya"