This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2pde
From Proteopedia
(Difference between revisions)
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:2pde.png|left|200px]] | ||
| - | < | + | ==THE HIGH RESOLUTION STRUCTURE OF THE PERIPHERAL SUBUNIT-BINDING DOMAIN OF DIHYDROLIPOAMIDE ACETYLTRANSFERASE FROM THE PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX OF BACILLUS STEAROTHERMOPHILUS== |
| - | + | <StructureSection load='2pde' size='340' side='right'caption='[[2pde]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2pde]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PDE FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2pde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pde OCA], [https://pdbe.org/2pde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pde RCSB], [https://www.ebi.ac.uk/pdbsum/2pde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pde ProSAT]</span></td></tr> | |
| - | + | </table> | |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). | ||
| + | == 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/pd/2pde_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=2pde ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Appella E]] | |
| - | + | [[Category: Brocklehurst SM]] | |
| - | + | [[Category: Hipps DS]] | |
| - | + | [[Category: Kalia YN]] | |
| - | + | [[Category: Perham RN]] | |
| - | + | [[Category: Sakaguchi K]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | [[Category: | + | |
| - | [[Category: Appella | + | |
| - | [[Category: Brocklehurst | + | |
| - | [[Category: Hipps | + | |
| - | [[Category: Kalia | + | |
| - | [[Category: Perham | + | |
| - | [[Category: Sakaguchi | + | |
| - | + | ||
| - | + | ||
Current revision
THE HIGH RESOLUTION STRUCTURE OF THE PERIPHERAL SUBUNIT-BINDING DOMAIN OF DIHYDROLIPOAMIDE ACETYLTRANSFERASE FROM THE PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX OF BACILLUS STEAROTHERMOPHILUS
| |||||||||||
