1ope: Difference between revisions

Revision as of 15:20, 21 February 2008

Deletion mutant of SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEART

OverviewOverview

Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5) activates the acetoacetate in ketone bodies by transferring the CoA group from succinyl-CoA to acetoacetate to produce acetoacetyl-CoA and succinate. In the reaction, a glutamate residue at the active site of the enzyme forms a thioester bond with CoA and in this form the enzyme is subject to autolytic fragmentation. The crystal structure of pig heart SCOT has been solved and refined to 1.7 A resolution in a new crystal form. The structure shows the active-site glutamate residue in a conformation poised for autolytic fragmentation, with its side chain accepting one hydrogen bond from Asn281 and another from its own amide N atom. However, the conformation of this glutamate side chain would have to change for the residues that are conserved in the CoA transferases (Gln99, Gly386 and Ala387) to participate in stabilizing the tetrahedral transition states of the catalytic mechanism. The structures of a deletion mutant in two different crystal forms were also solved.

About this StructureAbout this Structure

1OPE is a Single protein structure of sequence from Sus scrofa with and as ligands. Active as 3-oxoacid CoA-transferase, with EC number 2.8.3.5 Full crystallographic information is available from OCA.

ReferenceReference

Structure of the CoA transferase from pig heart to 1.7 A resolution., Coros AM, Swenson L, Wolodko WT, Fraser ME, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1717-25. Epub 2004, Sep 23. PMID:15388917

Page seeded by OCA on Thu Feb 21 14:20:09 2008

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OCA

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-[[Image:1ope.jpg|left|200px]]<br /><applet load="1ope" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ope.jpg|left|200px]]<br /><applet load="1ope" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ope, resolution 2.50&Aring;" />
 '''Deletion mutant of SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEART'''<br />
 ==Overview==
-Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5) activates the, acetoacetate in ketone bodies by transferring the CoA group from, succinyl-CoA to acetoacetate to produce acetoacetyl-CoA and succinate. In, the reaction, a glutamate residue at the active site of the enzyme forms a, thioester bond with CoA and in this form the enzyme is subject to, autolytic fragmentation. The crystal structure of pig heart SCOT has been, solved and refined to 1.7 A resolution in a new crystal form. The, structure shows the active-site glutamate residue in a conformation poised, for autolytic fragmentation, with its side chain accepting one hydrogen, bond from Asn281 and another from its own amide N atom. However, the, conformation of this glutamate side chain would have to change for the, residues that are conserved in the CoA transferases (Gln99, Gly386 and, Ala387) to participate in stabilizing the tetrahedral transition states of, the catalytic mechanism. The structures of a deletion mutant in two, different crystal forms were also solved.
+Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5) activates the acetoacetate in ketone bodies by transferring the CoA group from succinyl-CoA to acetoacetate to produce acetoacetyl-CoA and succinate. In the reaction, a glutamate residue at the active site of the enzyme forms a thioester bond with CoA and in this form the enzyme is subject to autolytic fragmentation. The crystal structure of pig heart SCOT has been solved and refined to 1.7 A resolution in a new crystal form. The structure shows the active-site glutamate residue in a conformation poised for autolytic fragmentation, with its side chain accepting one hydrogen bond from Asn281 and another from its own amide N atom. However, the conformation of this glutamate side chain would have to change for the residues that are conserved in the CoA transferases (Gln99, Gly386 and Ala387) to participate in stabilizing the tetrahedral transition states of the catalytic mechanism. The structures of a deletion mutant in two different crystal forms were also solved.
 ==About this Structure==
-OPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with HG and K as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-oxoacid_CoA-transferase 3-oxoacid CoA-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.5 2.8.3.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OPE OCA].
+OPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-oxoacid_CoA-transferase 3-oxoacid CoA-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.5 2.8.3.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPE OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Sus scrofa]]
-[[Category: Coros, A.M.]]
+[[Category: Coros, A M.]]
-[[Category: Fraser, M.E.]]
+[[Category: Fraser, M E.]]
 [[Category: Swenson, L.]]
-[[Category: Wolodko, W.T.]]
+[[Category: Wolodko, W T.]]
 [[Category: HG]]
 [[Category: K]]
 [[Category: alpha/beta protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:05:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:09 2008''