1jeh

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(New page: 200px<br /><applet load="1jeh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jeh, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1jeh.jpg|left|200px]]<br /><applet load="1jeh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jeh, resolution 2.40&Aring;" />
caption="1jeh, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE'''<br />
'''CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE'''<br />
==Overview==
==Overview==
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The crystal structure of eucaryotic lipoamide dehydrogenase from yeast has, been determined by an X-ray analysis at 2.7 (partially at 2.4) A, resolution. The enzyme has two identical subunits related by a pseudo, twofold symmetry. The tertiary structure is similar to those of other, procaryotic enzymes. The active site, consisting of FAD, Cys44, and Cys49, from one subunit and His457' from the other subunit, is highly conserved., This enzyme is directly bound to the core protein E2 of the 2-oxoglutarate, dehydrogenase complex, whereas it is bound to the pyruvate dehydrogenase, complex through a protein X. The calculated electrostatic potential, suggests two characteristic regions for binding with these two proteins.
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The crystal structure of eucaryotic lipoamide dehydrogenase from yeast has been determined by an X-ray analysis at 2.7 (partially at 2.4) A resolution. The enzyme has two identical subunits related by a pseudo twofold symmetry. The tertiary structure is similar to those of other procaryotic enzymes. The active site, consisting of FAD, Cys44, and Cys49 from one subunit and His457' from the other subunit, is highly conserved. This enzyme is directly bound to the core protein E2 of the 2-oxoglutarate dehydrogenase complex, whereas it is bound to the pyruvate dehydrogenase complex through a protein X. The calculated electrostatic potential suggests two characteristic regions for binding with these two proteins.
==About this Structure==
==About this Structure==
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1JEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JEH OCA].
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1JEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEH OCA].
==Reference==
==Reference==
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Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast., Toyoda T, Suzuki K, Sekiguchi T, Reed LJ, Takenaka A, J Biochem (Tokyo). 1998 Apr;123(4):668-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9538259 9538259]
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Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast., Toyoda T, Suzuki K, Sekiguchi T, Reed LJ, Takenaka A, J Biochem. 1998 Apr;123(4):668-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9538259 9538259]
[[Category: Dihydrolipoyl dehydrogenase]]
[[Category: Dihydrolipoyl dehydrogenase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: pyruvate dehydrogenase complex]]
[[Category: pyruvate dehydrogenase complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:10:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:45 2008''

Revision as of 11:21, 21 February 2008


1jeh, resolution 2.40Å

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CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE

Overview

The crystal structure of eucaryotic lipoamide dehydrogenase from yeast has been determined by an X-ray analysis at 2.7 (partially at 2.4) A resolution. The enzyme has two identical subunits related by a pseudo twofold symmetry. The tertiary structure is similar to those of other procaryotic enzymes. The active site, consisting of FAD, Cys44, and Cys49 from one subunit and His457' from the other subunit, is highly conserved. This enzyme is directly bound to the core protein E2 of the 2-oxoglutarate dehydrogenase complex, whereas it is bound to the pyruvate dehydrogenase complex through a protein X. The calculated electrostatic potential suggests two characteristic regions for binding with these two proteins.

About this Structure

1JEH is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Dihydrolipoyl dehydrogenase, with EC number 1.8.1.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast., Toyoda T, Suzuki K, Sekiguchi T, Reed LJ, Takenaka A, J Biochem. 1998 Apr;123(4):668-74. PMID:9538259

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