From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2fpp.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2fpp.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2fpp| PDB=2fpp | SCENE= }} | | {{STRUCTURE_2fpp| PDB=2fpp | SCENE= }} |
| | | | |
| - | '''Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16481318}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16481318 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16481318}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Ryan, D G.]] | | [[Category: Ryan, D G.]] |
| | [[Category: Active site phosphohistidine residue]] | | [[Category: Active site phosphohistidine residue]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:10:31 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:33:01 2008'' |
Revision as of 16:33, 28 July 2008
Template:STRUCTURE 2fpp
Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions
Template:ABSTRACT PUBMED 16481318
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
Page seeded by OCA on Mon Jul 28 19:33:01 2008
