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3e3z

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{{Seed}}
 
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[[Image:3e3z.png|left|200px]]
 
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==Crystal structure of bovine coupling Factor B bound with phenylarsine oxide==
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The line below this paragraph, containing "STRUCTURE_3e3z", creates the "Structure Box" on the page.
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<StructureSection load='3e3z' size='340' side='right'caption='[[3e3z]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3e3z]] 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=3E3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E3Z FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.7&#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=PA0:PHENYLARSINE+OXIDE'>PA0</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_3e3z| PDB=3e3z | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e3z OCA], [https://pdbe.org/3e3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e3z RCSB], [https://www.ebi.ac.uk/pdbsum/3e3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e3z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/3e3z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3e3z ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of bovine coupling Factor B bound with phenylarsine oxide===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18768789}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3e3z" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18768789 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18768789}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3E3Z 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=3E3Z OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18768789 18768789]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Belogrudov, G I.]]
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[[Category: Belogrudov GI]]
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[[Category: Lee, J K.]]
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[[Category: Lee JK]]
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[[Category: Stroud, R M.]]
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[[Category: Stroud RM]]
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[[Category: Cf0]]
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[[Category: Electron transport]]
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[[Category: Hydrogen ion transport]]
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[[Category: Inner membrane]]
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[[Category: Ion transport]]
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[[Category: Leucine-rich repeat]]
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[[Category: Membrane]]
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[[Category: Mitochondrion]]
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[[Category: Transit peptide]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 24 09:13:42 2008''
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Current revision

Crystal structure of bovine coupling Factor B bound with phenylarsine oxide

PDB ID 3e3z

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