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[[Image:1eud.jpg|left|200px]]<br /><applet load="1eud" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1eud, resolution 2.1&Aring;" />
'''CRYSTAL STRUCTURE OF PHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF PHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE==
Succinyl-CoA synthetase (SCS) catalyzes the reversible phosphorylation/dephosphorylation reaction: inverted question mark inverted question mark inverted question markrm succinyl inverted question markhbox inverted question mark- inverted question markCoA+NDP+P_i inverted question markleftrightarrow succinate+CoA+NTP inverted question mark inverted question markwhere N denotes adenosine or guanosine. In the course of the reaction, an essential histidine residue is transiently phosphorylated. We have crystallized and solved the structure of the GTP-specific isoform of SCS from pig heart (EC 6.2.1.4) in both the dephosphorylated and phosphorylated forms. The structures were refined to 2.1 A resolution. In the dephosphorylated structure, the enzyme is stabilized via coordination of a phosphate ion by the active-site histidine residue and the two "power" helices, one contributed by each subunit of the alphabeta-dimer. Small changes in the conformations of residues at the amino terminus of the power helix contributed by the alpha-subunit allow the enzyme to accommodate either the covalently bound phosphoryl group or the free phosphate ion. Structural comparisons are made between the active sites in these two forms of the enzyme, both of which can occur along the catalytic path. Comparisons are also made with the structure of Escherichia coli SCS. The domain that has been shown to bind ADP in E. coli SCS is more open in the pig heart, GTP-specific SCS structure.
<StructureSection load='1eud' size='340' side='right'caption='[[1eud]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1eud]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1eud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eud OCA], [https://pdbe.org/1eud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eud RCSB], [https://www.ebi.ac.uk/pdbsum/1eud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eud ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUCA_PIG SUCA_PIG] Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity).
== 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/eu/1eud_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=1eud ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EUD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Succinate--CoA_ligase_(GDP-forming) Succinate--CoA ligase (GDP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.4 6.2.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUD OCA].
*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase., Fraser ME, James MN, Bridger WA, Wolodko WT, J Mol Biol. 2000 Jun 23;299(5):1325-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10873456 10873456]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Succinate--CoA ligase (GDP-forming)]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Bridger, W A.]]
[[Category: Bridger WA]]
[[Category: Fraser, M E.]]
[[Category: Fraser ME]]
[[Category: James, M N.G.]]
[[Category: James MNG]]
[[Category: Wolodko, W T.]]
[[Category: Wolodko WT]]
[[Category: SO4]]
[[Category: gtp-specific]]
[[Category: ligase]]
[[Category: phosphonohistidine]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:35 2008''

Latest revision as of 10:06, 20 March 2024

CRYSTAL STRUCTURE OF PHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE

1eud, resolution 2.10Å

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