3oeh
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Structure of four mutant forms of yeast F1 ATPase: beta-V279F== | |
| - | + | <StructureSection load='3oeh' size='340' side='right' caption='[[3oeh]], [[Resolution|resolution]] 3.00Å' scene=''> | |
| - | === | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3oeh]] is a 27 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OEH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OEH FirstGlance]. <br> | |
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hld|2hld]], [[3fks|3fks]], [[1w0j|1w0j]], [[3oe7|3oe7]], [[3oee|3oee]], [[3ofn|3ofn]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATP1, YBL099W, YBL0827 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), ATP2, YJR121W, J2041 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), ATP3, ATP3a, ATP3b, YBR039W, YBR0408 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), ATP16, YDL004W, YD8119.03, D2935 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), ATP15, YPL271W, P0345 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oeh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oeh RCSB], [http://www.ebi.ac.uk/pdbsum/3oeh PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/oe/3oeh_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mitochondrial ATP synthase couples the flow of protons with the phosphorylation of ADP. A class of mutations, the mitochondrial genome integrity (mgi) mutations, has been shown to uncouple this process in the yeast mitochondrial ATP synthase. Four mutant forms of the yeast F(1) ATPase with mgi mutations were crystallized; the structures were solved and analyzed. The analysis identifies two mechanisms of structural uncoupling: one in which the empty catalytic site is altered and in doing so, apparently disrupts substrate (phosphate) binding, and a second where the steric hindrance predicted between gammaLeu83 and beta(DP) residues, Leu391 and Glu395, located in Catch 2 region, is reduced allowing rotation of the gamma-subunit with less impedance. Overall, the structures provide key insights into the critical interactions in the yeast ATP synthase involved in the coupling process. | ||
| - | + | Crystal structures of mutant forms of the yeast F1 ATPase reveal two modes of uncoupling.,Arsenieva D, Symersky J, Wang Y, Pagadala V, Mueller DM J Biol Chem. 2010 Sep 14. PMID:20843806<ref>PMID:20843806</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[ATPase|ATPase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Arsenieva, D | + | [[Category: Arsenieva, D]] |
| - | [[Category: Mueller, D M | + | [[Category: Mueller, D M]] |
| - | [[Category: Pagadala, V | + | [[Category: Pagadala, V]] |
| - | [[Category: Symersky, J | + | [[Category: Symersky, J]] |
| - | [[Category: Wang, Y | + | [[Category: Wang, Y]] |
[[Category: Adp]] | [[Category: Adp]] | ||
[[Category: Atp phosphatase]] | [[Category: Atp phosphatase]] | ||
Revision as of 08:33, 18 December 2014
Structure of four mutant forms of yeast F1 ATPase: beta-V279F
| |||||||||||
