2g67

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{{Seed}}
 
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[[Image:2g67.png|left|200px]]
 
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==E. Coli Pyruvate Dehydrogenase E1 Component (Apoenzyme)==
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The line below this paragraph, containing "STRUCTURE_2g67", creates the "Structure Box" on the page.
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<StructureSection load='2g67' size='340' side='right'caption='[[2g67]], [[Resolution|resolution]] 2.32&Aring;' 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'>[[2g67]] 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=2G67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G67 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">X-ray diffraction, [[Resolution|Resolution]] 2.32&#8491;</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=2g67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g67 OCA], [https://pdbe.org/2g67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g67 RCSB], [https://www.ebi.ac.uk/pdbsum/2g67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g67 ProSAT]</span></td></tr>
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{{STRUCTURE_2g67| PDB=2g67 | SCENE= }}
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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/g6/2g67_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=2g67 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 first enzymatic component, E1 (EC 1.2.4.1), of the pyruvate dehydrogenase multienzyme complex (PDHc) utilizes thiamine diphosphate (ThDP) and Mg(2+) as cofactors. The structure of a branched-chain-specific E1 apoenzyme from the heterotetrameric alpha(2)beta(2) E1 family was recently reported and showed that disorder-to-order transformations in two active-site loops take place upon cofactor binding. To ascertain what effect the absence of cofactor may have in the homodimeric alpha(2) Escherichia coli PDHc E1, the corresponding apoenzyme has been prepared and its three-dimensional structure determined and analyzed at 2.32 A by crystallographic methods. This represents the first reported apoenzyme structure for any E1 component from the homodimeric alpha(2) family. Electron-density features occurring in the region where the cofactor pyrimidine ring would normally be expected to bind are of size, shape and location compatible with water molecules that form a hydrogen-bonded linkage between residues Glu571 and Val192, which normally make conserved interactions with the ThDP cofactor. A histidine side chain that normally forms hydrogen bonds to ThDP is disordered in its absence and partially occupies two sites. Unlike in the reported heterotetrameric branched-chain apo-E1, no disorder/order loop transformations are evident in apo-PDHc E1 relative to the holo-E1 enzyme (PDHc E1-ThDP-Mg(2+)). Differences in the extent of hydrogen-bonding networks found in the apo-E1 enzyme, the holo-E1 enzyme and in an inhibitor complex with bound thiamine 2-thiazolone diphosphate (ThTDP), PDHc E1-ThTDP-Mg(2+), are described.
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===E. Coli Pyruvate Dehydrogenase E1 Component (Apoenzyme)===
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Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution.,Chandrasekhar K, Arjunan P, Sax M, Nemeria N, Jordan F, Furey W Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1382-6. Epub 2006, Oct 18. PMID:17057342<ref>PMID:17057342</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 2g67" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17057342}}, adds the Publication Abstract to the page
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*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17057342 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17057342}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2G67 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G67 OCA].
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==Reference==
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<ref group="xtra">PMID:17057342</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Arjunan, P.]]
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[[Category: Large Structures]]
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[[Category: Chandrasekhar, K.]]
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[[Category: Arjunan P]]
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[[Category: Furey, W.]]
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[[Category: Chandrasekhar K]]
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[[Category: Apoenzyme]]
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[[Category: Furey W]]
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[[Category: Homodimer]]
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[[Category: Pyruvate dehydrogenase e1 component]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:17:07 2009''
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Current revision

E. Coli Pyruvate Dehydrogenase E1 Component (Apoenzyme)

PDB ID 2g67

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