3e4g: Difference between revisions

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==Crystal structure of bovine coupling Factor B, G28E mutant==
The line below this paragraph, containing "STRUCTURE_3e4g", creates the "Structure Box" on the page.
<StructureSection load='3e4g' size='340' side='right'caption='[[3e4g]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3e4g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4G 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]] 0.96&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
{{STRUCTURE_3e4g|  PDB=3e4g  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4g OCA], [https://pdbe.org/3e4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4g RCSB], [https://www.ebi.ac.uk/pdbsum/3e4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATP5S_BOVIN ATP5S_BOVIN] Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway.<ref>PMID:12361715</ref> <ref>PMID:18768789</ref>
== 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/e4/3e4g_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=3e4g ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Coupling factor B (FB) is a mitochondrial inner membrane polypeptide that facilitates the energy-driven catalysis of ATP synthesis in animal mitochondria by blocking a proton leak across the membrane. Here, we report the crystal structure of the bovine mitochondrial FB mutant with Gly-3-Glu substitution determined at a resolution of 0.96 A and that of the WT polypeptide at a resolution of 2.9 A. The structure reveals an oblong, oval-shaped molecule with a unique globular N-terminal domain that is proposed to be the membrane anchor domain and the capping region to the C-terminal leucine-rich repeats domain. A short N-terminal alpha-helix, which extends away from the molecule's body, is suggestive of functioning as an anchor for FB to the matrix side of the mitochondrial inner membrane. Identification of a bound Mg(2+) ion reveals that FB is a metalloprotein. We also report the cocrystal structures of FB bound with phenylarsine oxide and Cd(2+), two known inhibitors of the FB coupling activity.


===Crystal structure of bovine coupling Factor B, G28E mutant===
Crystal structure of bovine mitochondrial factor B at 0.96-A resolution.,Lee JK, Belogrudov GI, Stroud RM Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13379-84. Epub 2008 Sep 3. PMID:18768789<ref>PMID:18768789</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
3E4G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E4G OCA].
<div class="pdbe-citations 3e4g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Belogrudov, G I.]]
[[Category: Belogrudov GI]]
[[Category: Lee, J K.]]
[[Category: Lee JK]]
[[Category: Stroud, R M.]]
[[Category: Stroud RM]]
[[Category: Cf0]]
[[Category: Electron transport]]
[[Category: Hydrogen ion transport]]
[[Category: Inner membrane]]
[[Category: Ion transport]]
[[Category: Leucine-rich repeat]]
[[Category: Membrane]]
[[Category: Mitochondrion]]
[[Category: Transit peptide]]
[[Category: Transport]]
 
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