1pmr

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(New page: 200px<br /><applet load="1pmr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pmr" /> '''LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINY...)
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[[Image:1pmr.gif|left|200px]]<br /><applet load="1pmr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pmr" />
 
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'''LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE COMPONENT OF THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI, NMR, 25 STRUCTURES'''<br />
 
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==Overview==
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==LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE COMPONENT OF THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI, NMR, 25 STRUCTURES==
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A sub-gene encoding the lipoyl domain of the dihydrolipoyl, succinyltransferase polypeptide chain of the 2-oxoglutarate dehydrogenase, multienzyme complex of Escherichia coli was over-expressed and the protein, was purified uniformly labelled with 15N. The three-dimensional structure, of the domain was determined by means of nuclear magnetic resonance, spectroscopy, based on 905 nuclear Overhauser effect inter-proton distance, restraints, 42 phi torsion angle restraints and hydrogen bond restraints, from 24 slowly exchanging amide protons. The structure of the 80-residue, domain is that of a flattened beta-barrel surrounding a hydrophobic core, in which Trp22 plays a central role in anchoring two four-stranded sheets, together. The polypeptide backbone exhibits a 2-fold axis of, quasi-symmetry, with the lipoylation site, Lys43, located at the tip of an, exposed beta-turn in one beta-sheet and the N and C-terminal residues, close together in space in the other beta-sheet. The atomic r.m.s., distribution about the mean coordinate is 0.46 A for the backbone atoms in, the highly structured region and 0.88 A along the entire backbone, (residues Ser1 to Asn80), including a less well-defined surface loop and, the lipoyl-lysine beta-turn. The structure closely resembles that of the, lipoyl domains from pyruvate dehydrogenase complexes, in accord with the, existence of strongly conserved residues at critical positions in the, domains. The structures of the lipoyl domains throw light on the, requirements for the specificity of reductive acylation of their pendant, lipoyl groups in the parent 2-oxo acid dehydrogenase complexes; an, important aspect of the mechanisms underlying active site coupling and, substrate channelling.
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<StructureSection load='1pmr' size='340' side='right'caption='[[1pmr]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pmr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The October 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Citric Acid Cycle'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_10 10.2210/rcsb_pdb/mom_2012_10]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PMR FirstGlance]. <br>
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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=1pmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmr OCA], [https://pdbe.org/1pmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pmr RCSB], [https://www.ebi.ac.uk/pdbsum/1pmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pmr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (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/pm/1pmr_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=1pmr ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1PMR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PMR OCA].
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*[[2-oxoglutarate dehydrogenase 3D structures|2-oxoglutarate dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli., Ricaud PM, Howard MJ, Roberts EL, Broadhurst RW, Perham RN, J Mol Biol. 1996 Nov 22;264(1):179-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8950276 8950276]
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[[Category: Citric Acid Cycle]]
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[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Broadhurst, R.W.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Howard, M.J.]]
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[[Category: Broadhurst RW]]
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[[Category: Perham, R.N.]]
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[[Category: Howard MJ]]
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[[Category: Ricaud, P.M.]]
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[[Category: Perham RN]]
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[[Category: Roberts, E.L.]]
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[[Category: Ricaud PM]]
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[[Category: 2-oxoglutarate dehydrogenase]]
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[[Category: Roberts EL]]
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[[Category: complex]]
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[[Category: glycolysis]]
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[[Category: lipoyl domain]]
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[[Category: nmr]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:55:43 2007''
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Current revision

LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE COMPONENT OF THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI, NMR, 25 STRUCTURES

PDB ID 1pmr

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