2fp4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2fp4.gif|left|200px]]
{{Seed}}
[[Image:2fp4.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2fp4|  PDB=2fp4  |  SCENE=  }}  
{{STRUCTURE_2fp4|  PDB=2fp4  |  SCENE=  }}  


'''Crystal structure of pig GTP-specific succinyl-CoA synthetase in complex with GTP'''
===Crystal structure of pig GTP-specific succinyl-CoA synthetase in complex with GTP===




==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 24: Line 28:
[[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 Sun May  4 04:09:37 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:18:51 2008''

Revision as of 21:18, 27 July 2008

File:2fp4.png

Template:STRUCTURE 2fp4

Crystal structure of pig GTP-specific succinyl-CoA synthetase in complex with GTP

Template:ABSTRACT PUBMED 16481318

About this Structure

2FP4 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 00:18:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2fp4&oldid=673132"