2fpp
From Proteopedia
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| - | [[Image:2fpp.gif|left|200px]] | + | [[Image:2fpp.gif|left|200px]] |
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| - | '''Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions''' | + | {{Structure |
| + | |PDB= 2fpp |SIZE=350|CAPTION= <scene name='initialview01'>2fpp</scene>, resolution 2.350Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</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= SUCLG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]), SUCLG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FPP is a [ | + | 2FPP 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=2FPP OCA]. |
==Reference== | ==Reference== | ||
| - | Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetase., Fraser ME, Hayakawa K, Hume MS, Ryan DG, Brownie ER, J Biol Chem. 2006 Apr 21;281(16):11058-65. Epub 2006 Feb 15. PMID:[http:// | + | Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetase., Fraser ME, Hayakawa K, Hume MS, Ryan DG, Brownie ER, J Biol Chem. 2006 Apr 21;281(16):11058-65. Epub 2006 Feb 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16481318 16481318] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Succinate--CoA ligase (GDP-forming)]] | [[Category: Succinate--CoA ligase (GDP-forming)]] | ||
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[[Category: active site phosphohistidine residue]] | [[Category: active site phosphohistidine residue]] | ||
| - | ''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 16:55:18 2008'' |
Revision as of 14:55, 20 March 2008
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| , resolution 2.350Å | |||||||
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| Ligands: | and | ||||||
| Gene: | SUCLG1 (Sus scrofa), SUCLG2 (Sus scrofa) | ||||||
| Activity: | Succinate--CoA ligase (GDP-forming), with EC number 6.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions
Overview
Two isoforms of succinyl-CoA synthetase exist in mammals, one specific for ATP and the other for GTP. The GTP-specific form of pig succinyl-CoA synthetase has been crystallized in the presence of GTP and the structure determined to 2.1 A resolution. GTP is bound in the ATP-grasp domain, where interactions of the guanine base with a glutamine residue (Gln-20beta) and with backbone atoms provide the specificity. The gamma-phosphate interacts with the side chain of an arginine residue (Arg-54beta) and with backbone amide nitrogen atoms, leading to tight interactions between the gamma-phosphate and the protein. This contrasts with the structures of ATP bound to other members of the family of ATP-grasp proteins where the gamma-phosphate is exposed, free to react with the other substrate. To test if GDP would interact with GTP-specific succinyl-CoA synthetase in the same way that ADP interacts with other members of the family of ATP-grasp proteins, the structure of GDP bound to GTP-specific succinyl-CoA synthetase was also determined. A comparison of the conformations of GTP and GDP shows that the bases adopt the same position but that changes in conformation of the ribose moieties and the alpha- and beta-phosphates allow the gamma-phosphate to interact with the arginine residue and amide nitrogen atoms in GTP, while the beta-phosphate interacts with these residues in GDP. The complex of GTP with succinyl-CoA synthetase shows that the enzyme is able to protect GTP from hydrolysis when the active-site histidine residue is not in position to be phosphorylated.
About this Structure
2FPP is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetase., Fraser ME, Hayakawa K, Hume MS, Ryan DG, Brownie ER, J Biol Chem. 2006 Apr 21;281(16):11058-65. Epub 2006 Feb 15. PMID:16481318
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