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New page: left|200px<br /><applet load="1lab" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lab" /> '''THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DO...
 
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[[Image:1lab.jpg|left|200px]]<br /><applet load="1lab" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lab" />
'''THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX'''<br />


==Overview==
==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==
The structure of the lipoyl domain from the pyruvate dehydrogenase, multienzyme complex of Bacillus stearothermophilus has been determined by, means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear, Overhauser effect distance constraints and 76 dihedral angle restraints, were employed as the input for the structure calculations, which were, performed using a hybrid distance geometry-simulated annealing strategy, and the programs DISGEO and X-PLOR. The overall structure of the lipoyl, domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase, polypeptide chain) is that of a flattened eight-stranded beta-barrel, folded around a core of well-defined hydrophobic residues. The lipoylation, site, lysine 42, is located in the middle of a beta-turn, and the N and, C-terminal residues of the domain are close together in adjacent, beta-strands at the opposite end of the molecule. The polypeptide backbone, exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of, residues 15 to 39 and 52 to 76 being almost superimposable on those of, residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation =, 1.48 A). The amino acid residues at key positions in the structure are, conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.
<StructureSection load='1lab' size='340' side='right'caption='[[1lab]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAB 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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [https://pdbe.org/1lab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [https://www.ebi.ac.uk/pdbsum/1lab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lab 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/la/1lab_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=1lab ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].
*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex., Dardel F, Davis AL, Laue ED, Perham RN, J Mol Biol. 1993 Feb 20;229(4):1037-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8445635 8445635]
[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dardel, F.]]
[[Category: Dardel F]]
[[Category: Davis, A.L.]]
[[Category: Davis AL]]
[[Category: Laue, E.D.]]
[[Category: Laue ED]]
[[Category: Perham, R.N.]]
[[Category: Perham RN]]
[[Category: transferase (acyltransferase)]]
 
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Retrieved from "https://proteopedia.org/1lab"