2fyo
From Proteopedia
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| - | [[Image:2fyo.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of rat carnitine palmitoyltransferase 2 in space group P43212== |
| - | + | <StructureSection load='2fyo' size='340' side='right'caption='[[2fyo]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2fyo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYO FirstGlance]. <br> | |
| - | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fw3|2fw3]], [[2deb|2deb]]</div></td></tr> |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carnitine_O-palmitoyltransferase Carnitine O-palmitoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.21 2.3.1.21] </span></td></tr> | |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyo OCA], [https://pdbe.org/2fyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyo RCSB], [https://www.ebi.ac.uk/pdbsum/2fyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyo ProSAT]</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/fy/2fyo_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=2fyo ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Carnitine palmitoyltransferases (CPTs) are part of the enzymatic system that imports fatty acids into mitochondria. The crystal structure of rat CPT-2 by Rufer et al. (2006) (this issue of Structure) reveals a Y-shaped tunnel for binding the CoA and acyl-carnitine substrates and a hydrophobic insert mediating membrane association. | ||
| - | + | A monotopic membrane protein goes solo.,Mattevi A Structure. 2006 Apr;14(4):628-9. PMID:16615901<ref>PMID:16615901</ref> | |
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| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2fyo" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Carnitine palmitoyltransferase|Carnitine palmitoyltransferase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Buffalo rat]] | ||
[[Category: Carnitine O-palmitoyltransferase]] | [[Category: Carnitine O-palmitoyltransferase]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Banner, D W]] | |
| - | [[Category: Banner, D W | + | [[Category: Benz, J]] |
| - | [[Category: Benz, J | + | [[Category: Chomienne, O]] |
| - | [[Category: Chomienne, O | + | [[Category: Gsell, B]] |
| - | [[Category: Gsell, B | + | [[Category: Hennig, M]] |
| - | [[Category: Hennig, M | + | [[Category: Mueller, F]] |
| - | [[Category: Mueller, F | + | [[Category: Roo, E De]] |
| - | [[Category: Roo, E De | + | [[Category: Rufer, A C]] |
| - | [[Category: Rufer, A C | + | [[Category: Stihle, M]] |
| - | [[Category: Stihle, M | + | [[Category: Thoma, R]] |
| - | [[Category: Thoma, R | + | |
[[Category: Central six-stranded beta-sheet]] | [[Category: Central six-stranded beta-sheet]] | ||
| - | + | [[Category: Transferase]] | |
Current revision
Crystal structure of rat carnitine palmitoyltransferase 2 in space group P43212
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