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2fpi
From Proteopedia
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|PDB= 2fpi |SIZE=350|CAPTION= <scene name='initialview01'>2fpi</scene>, resolution 2.700Å | |PDB= 2fpi |SIZE=350|CAPTION= <scene name='initialview01'>2fpi</scene>, resolution 2.700Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]], [[2fp4|2FP4]], [[2fpg|2FPG]], [[2fpp|2FPP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpi OCA], [http://www.ebi.ac.uk/pdbsum/2fpi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fpi RCSB]</span> | ||
}} | }} | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Fraser, M E.]] | [[Category: Fraser, M E.]] | ||
| - | [[Category: SO4]] | ||
[[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 03:05:59 2008'' |
Revision as of 00:06, 31 March 2008
| |||||||
| , resolution 2.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SUCLG1 (Sus scrofa), SUCLG2 (Sus scrofa) | ||||||
| Activity: | Succinate--CoA ligase (GDP-forming), with EC number 6.2.1.4 | ||||||
| Related: | 1EUC, 1EUD, 2FP4, 2FPG, 2FPP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol
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
2FPI 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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