1iyv

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{{Seed}}
 
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[[Image:1iyv.png|left|200px]]
 
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==LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, 29 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1iyv", creates the "Structure Box" on the page.
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<StructureSection load='1iyv' size='340' side='right'caption='[[1iyv]]' 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'>[[1iyv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYV 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">Solution NMR</td></tr>
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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=1iyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyv OCA], [https://pdbe.org/1iyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyv RCSB], [https://www.ebi.ac.uk/pdbsum/1iyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyv ProSAT]</span></td></tr>
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{{STRUCTURE_1iyv| PDB=1iyv | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ODP2_AZOVI ODP2_AZOVI] 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).
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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/iy/1iyv_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=1iyv 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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The three-dimensional structure of the N-terminal lipoyl domain of the acetyltransferase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii has been determined using heteronuclear multidimensional NMR spectroscopy and dynamical simulated annealing. The structure is compared with the solution structure of the lipoyl domain of the A. vinelandii 2-oxoglutarate dehydrogenase complex. The overall fold of the two structures, described as a beta-barrel-sandwich hybrid, is very similar. This agrees well with the high similarity of NMR-derived parameters, e.g. chemical shifts, between the two lipoyl domains. The main structural differences between the two lipoyl domains occur in a solvent-exposed loop close in space to the lipoylation site. Despite their high structural similarity, these lipoyl domains show a high preference for being reductively acylated by their parent 2-oxo acid dehydrogenase. Potential residues of the lipoyl domain involved in this process of molecular recognition are discussed.
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===LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, 29 STRUCTURES===
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Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii.,Berg A, Vervoort J, de Kok A Eur J Biochem. 1997 Mar 1;244(2):352-60. PMID:9119000<ref>PMID:9119000</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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<div class="pdbe-citations 1iyv" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9119000}}, adds the Publication Abstract to the page
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*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9119000 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9119000}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1IYV is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYV OCA].
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==Reference==
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<ref group="xtra">PMID:9119000</ref><references group="xtra"/>
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[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
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[[Category: Large Structures]]
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[[Category: Berg, A.]]
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[[Category: Berg A]]
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[[Category: Kok, A De.]]
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[[Category: De Kok A]]
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[[Category: Vervoort, J.]]
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[[Category: Vervoort J]]
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[[Category: Acyltransferase]]
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[[Category: Glycolysis]]
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[[Category: Lipoyl]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 01:57:03 2009''
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Current revision

LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, 29 STRUCTURES

PDB ID 1iyv

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