1ege
From Proteopedia
(New page: 200px<br /> <applet load="1ege" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ege, resolution 2.75Å" /> '''STRUCTURE OF T255E,...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1EGE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with FAD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.3 1.3.99.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EGE OCA]]. | + | 1EGE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FAD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase Acyl-CoA dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.3 1.3.99.3]]. Structure known Active Sites: CA1, CA2, CA3 and CA4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EGE OCA]]. |
==Reference== | ==Reference== | ||
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity., Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ, Biochemistry. 1996 Sep 24;35(38):12412-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8823176 8823176] | Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity., Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ, Biochemistry. 1996 Sep 24;35(38):12412-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8823176 8823176] | ||
| + | [[Category: Acyl-CoA dehydrogenase]] | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ghisla, S.]] | [[Category: Ghisla, S.]] | ||
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[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:18:35 2007'' |
Revision as of 09:13, 30 October 2007
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STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE
Overview
Crystal structures of the wild type human medium-chain acyl-CoA, dehydrogenase (MCADH) and a double mutant in which its active center, base-arrangement has been altered to that of long chain acyl-CoA, dehydrogenase (LCADH), Glu376Gly/Thr255Glu, have been determined by X-ray, crystallography at 2.75 and 2.4 A resolution, respectively. The catalytic, base responsible for the alpha-proton abstraction from the thioester, substrate is Glu376 in MCADH, while that in LCADH is Glu255 (MCADH, numbering), located over 100 residues away in its primary amino acid, sequence. The structures of the mutant complexed with C8-, C12, and, C14-CoA have also been determined. The human enzyme structure is, essentially the same as that of the pig enzyme. The structure of the, mutant is unchanged upon ligand ... [(full description)]
About this Structure
1EGE is a [Single protein] structure of sequence from [Homo sapiens] with FAD as [ligand]. Active as [Acyl-CoA dehydrogenase], with EC number [1.3.99.3]. Structure known Active Sites: CA1, CA2, CA3 and CA4. Full crystallographic information is available from [OCA].
Reference
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity., Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ, Biochemistry. 1996 Sep 24;35(38):12412-20. PMID:8823176
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