1euc: Difference between revisions
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[[Image:1euc.gif|left|200px]] | [[Image:1euc.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF DEPHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE''' | {{Structure | ||
|PDB= 1euc |SIZE=350|CAPTION= <scene name='initialview01'>1euc</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF DEPHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EUC is a [ | 1EUC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUC OCA]. | ||
==Reference== | ==Reference== | ||
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:// | 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://www.ncbi.nlm.nih.gov/pubmed/10873456 10873456] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Succinate--CoA ligase (GDP-forming)]] | [[Category: Succinate--CoA ligase (GDP-forming)]] | ||
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[[Category: ligase]] | [[Category: ligase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:21 2008'' | ||
Revision as of 12:00, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | Succinate--CoA ligase (GDP-forming), with EC number 6.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF DEPHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE
OverviewOverview
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.
About this StructureAbout this Structure
1EUC is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
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:10873456
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