2fpp: Difference between revisions

Revision as of 18:23, 21 February 2008

Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions

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

2FPP is a Protein complex structure of sequences from Sus scrofa with and as ligands. Active as Succinate--CoA ligase (GDP-forming), with EC number 6.2.1.4 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

Page seeded by OCA on Thu Feb 21 17:23:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2fpp.gif|left|200px]]<br /><applet load="2fpp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2fpp.gif|left|200px]]<br /><applet load="2fpp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2fpp, resolution 2.350&Aring;" />
 '''Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions'''<br />
 ==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.
+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==
-FPP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4 and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FPP OCA].
+FPP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPP OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Succinate--CoA ligase (GDP-forming)]]
 [[Category: Sus scrofa]]
-[[Category: Brownie, E.R.]]
+[[Category: Brownie, E R.]]
-[[Category: Fraser, M.E.]]
+[[Category: Fraser, M E.]]
 [[Category: Hayakawa, K.]]
-[[Category: Hume, M.S.]]
+[[Category: Hume, M S.]]
-[[Category: Ryan, D.G.]]
+[[Category: Ryan, D G.]]
 [[Category: CL]]
 [[Category: SO4]]
 [[Category: active site phosphohistidine residue]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:41:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:51 2008''