2fp4: Difference between revisions
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|PDB= 2fp4 |SIZE=350|CAPTION= <scene name='initialview01'>2fp4</scene>, resolution 2.080Å | |PDB= 2fp4 |SIZE=350|CAPTION= <scene name='initialview01'>2fp4</scene>, resolution 2.080Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | |LIGAND= <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|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]) | |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]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1euc|1EUC]], [[1eud|1EUD]], [[2fpg|2FPG]], [[2fpi|2FPI]], [[2fpp|2FPP]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fp4 OCA], [http://www.ebi.ac.uk/pdbsum/2fp4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fp4 RCSB]</span> | |||
}} | }} | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Fraser, M E.]] | [[Category: Fraser, M E.]] | ||
[[Category: active site phosphohistidine residue]] | [[Category: active site phosphohistidine residue]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:53 2008'' | ||
Revision as of 03:05, 31 March 2008
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| , resolution 2.080Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | SUCLG1 (Sus scrofa), SUCLG2 (Sus scrofa) | ||||||
| Activity: | Succinate--CoA ligase (GDP-forming), with EC number 6.2.1.4 | ||||||
| Related: | 1EUC, 1EUD, 2FPG, 2FPI, 2FPP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of pig GTP-specific succinyl-CoA synthetase in complex with GTP
OverviewOverview
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 StructureAbout this Structure
2FP4 is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
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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