1m3e: Difference between revisions
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New page: left|200px<br /><applet load="1m3e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3e, resolution 2.5Å" /> '''Succinyl-COA:3-ketoac... |
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[[Image:1m3e.gif|left|200px]]<br /><applet load="1m3e" size=" | [[Image:1m3e.gif|left|200px]]<br /><applet load="1m3e" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1m3e, resolution 2.5Å" /> | caption="1m3e, resolution 2.5Å" /> | ||
'''Succinyl-COA:3-ketoacid COA transferase from pig heart (selenomethionine)'''<br /> | '''Succinyl-COA:3-ketoacid COA transferase from pig heart (selenomethionine)'''<br /> | ||
==Overview== | ==Overview== | ||
Ketoacidosis affects patients who are deficient in the enzyme activity of | Ketoacidosis affects patients who are deficient in the enzyme activity of succinyl-CoA:3-ketoacid CoA transferase (SCOT), since SCOT catalyses the activation of acetoacetate in the metabolism of ketone bodies. Thus far, structure/function analysis of the mammalian enzyme has been predicted based on the three-dimensional structure of a CoA transferase determined from an anaerobic bacterium that utilizes its enzyme for glutamate fermentation. To better interpret clinical data, we have determined the structure of a mammalian CoA transferase from pig heart by X-ray crystallography to 2.5 A resolution. Instrumental to the structure determination were selenomethionine substitution and the use of argon during purification and crystallization. Although pig heart SCOT adopts an alpha/beta protein fold, resembling the overall fold of the bacterial CoA transferase, several loops near the active site of pig heart SCOT follow different paths than the corresponding loops in the bacterial enzyme, accounting for differences in substrate specificities. Two missense mutations found associated with SCOT of ketoacidosis patients were mapped to a location in the structure that might disrupt the stabilization of the amino-terminal strand and thereby interfere with the proper folding of the protein into a functional enzyme. | ||
==About this Structure== | ==About this Structure== | ||
1M3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. 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:// | 1M3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. 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=1M3E OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Bateman, K | [[Category: Bateman, K S.]] | ||
[[Category: Brownie, E | [[Category: Brownie, E R.]] | ||
[[Category: Fraser, M | [[Category: Fraser, M E.]] | ||
[[Category: Wolodko, W | [[Category: Wolodko, W T.]] | ||
[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:07 2008'' | ||
