1l8a

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(New page: 200px<br /><applet load="1l8a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l8a, resolution 1.85&Aring;" /> '''E. COLI PYRUVATE DEH...)
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[[Image:1l8a.jpg|left|200px]]<br /><applet load="1l8a" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l8a, resolution 1.85&Aring;" />
 
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'''E. COLI PYRUVATE DEHYDROGENASE'''<br />
 
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==Overview==
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==E. COLI PYRUVATE DEHYDROGENASE==
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The crystal structure of the recombinant thiamin diphosphate-dependent E1, component from the Escherichia coli pyruvate dehydrogenase multienzyme, complex (PDHc) has been determined at a resolution of 1.85 A. The E. coli, PDHc E1 component E1p is a homodimeric enzyme and crystallizes with an, intact dimer in an asymmetric unit. Each E1p subunit consists of three, domains: N-terminal, middle, and C-terminal, with all having alpha/beta, folds. The functional dimer contains two catalytic centers located at the, interface between subunits. The ThDP cofactors are bound in the "V", conformation in clefts between the two subunits (binding involves the, N-terminal and middle domains), and there is a common ThDP binding fold., The cofactors are completely buried, as only the C2 atoms are accessible, from solution through the active site clefts. Significant structural, differences are observed between individual domains of E1p relative to, heterotetrameric multienzyme complex E1 components operating on branched, chain substrates. These differences may be responsible for reported, alternative E1p binding modes to E2 components within the respective, complexes. This paper represents the first structural example of a, functional pyruvate dehydrogenase E1p component from any species. It also, provides the first representative example for the entire family of, homodimeric (alpha2) E1 multienzyme complex components, and should serve, as a model for this class of enzymes.
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<StructureSection load='1l8a' size='340' side='right'caption='[[1l8a]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1l8a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L8A 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">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></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=1l8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8a OCA], [https://pdbe.org/1l8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l8a RCSB], [https://www.ebi.ac.uk/pdbsum/1l8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ODP1_ECOLI ODP1_ECOLI] Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
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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/l8/1l8a_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=1l8a 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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1L8A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and TDP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L8A OCA].
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*[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]]
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*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
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==Reference==
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__TOC__
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Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution., Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W, Biochemistry. 2002 Apr 23;41(16):5213-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11955070 11955070]
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Pyruvate dehydrogenase (acetyl-transferring)]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Arjunan P]]
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[[Category: Arjunan, P.]]
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[[Category: Furey W]]
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[[Category: Furey, W.]]
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[[Category: MG]]
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[[Category: TDP]]
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[[Category: alpha-keto acid dehydrogenase]]
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[[Category: pyruvate]]
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[[Category: thiamin diphosphate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:22:13 2007''
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E. COLI PYRUVATE DEHYDROGENASE

PDB ID 1l8a

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