1ebu

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(New page: 200px<br /><applet load="1ebu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ebu, resolution 2.60&Aring;" /> '''HOMOSERINE DEHYDROGE...)
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[[Image:1ebu.jpg|left|200px]]<br /><applet load="1ebu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ebu, resolution 2.60&Aring;" />
caption="1ebu, resolution 2.60&Aring;" />
'''HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE'''<br />
'''HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE'''<br />
==Overview==
==Overview==
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The structure of the antifungal drug target homoserine dehydrogenase (HSD), was determined from Saccharomyces cerevisiae in apo and holo forms, and as, a ternary complex with bound products, by X-ray diffraction. The three, forms show that the enzyme is a dimer, with each monomer composed of three, regions, the nucleotide-binding region, the dimerization region and the, catalytic region. The dimerization and catalytic regions have novel folds, whereas the fold of the nucleotide-binding region is a variation on the, Rossmann fold. The novel folds impose a novel composition and arrangement, of active site residues when compared to all other currently known, oxidoreductases. This observation, in conjunction with site-directed, mutagenesis of active site residues and steady-state kinetic measurements, suggest that HSD exhibits a new variation on dehydrogenase chemistry.
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The structure of the antifungal drug target homoserine dehydrogenase (HSD) was determined from Saccharomyces cerevisiae in apo and holo forms, and as a ternary complex with bound products, by X-ray diffraction. The three forms show that the enzyme is a dimer, with each monomer composed of three regions, the nucleotide-binding region, the dimerization region and the catalytic region. The dimerization and catalytic regions have novel folds, whereas the fold of the nucleotide-binding region is a variation on the Rossmann fold. The novel folds impose a novel composition and arrangement of active site residues when compared to all other currently known oxidoreductases. This observation, in conjunction with site-directed mutagenesis of active site residues and steady-state kinetic measurements, suggest that HSD exhibits a new variation on dehydrogenase chemistry.
==About this Structure==
==About this Structure==
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1EBU 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 NA, NDA and HSE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Homoserine_dehydrogenase Homoserine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.3 1.1.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EBU OCA].
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1EBU 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=NA:'>NA</scene>, <scene name='pdbligand=NDA:'>NDA</scene> and <scene name='pdbligand=HSE:'>HSE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Homoserine_dehydrogenase Homoserine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.3 1.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBU OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Berghuis, A.M.]]
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[[Category: Berghuis, A M.]]
[[Category: DeLaBarre, B.]]
[[Category: DeLaBarre, B.]]
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[[Category: Thompson, P.R.]]
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[[Category: Thompson, P R.]]
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[[Category: Wright, G.D.]]
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[[Category: Wright, G D.]]
[[Category: HSE]]
[[Category: HSE]]
[[Category: NA]]
[[Category: NA]]
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[[Category: ternary]]
[[Category: ternary]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:07 2008''

Revision as of 10:26, 21 February 2008


1ebu, resolution 2.60Å

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HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE

Overview

The structure of the antifungal drug target homoserine dehydrogenase (HSD) was determined from Saccharomyces cerevisiae in apo and holo forms, and as a ternary complex with bound products, by X-ray diffraction. The three forms show that the enzyme is a dimer, with each monomer composed of three regions, the nucleotide-binding region, the dimerization region and the catalytic region. The dimerization and catalytic regions have novel folds, whereas the fold of the nucleotide-binding region is a variation on the Rossmann fold. The novel folds impose a novel composition and arrangement of active site residues when compared to all other currently known oxidoreductases. This observation, in conjunction with site-directed mutagenesis of active site residues and steady-state kinetic measurements, suggest that HSD exhibits a new variation on dehydrogenase chemistry.

About this Structure

1EBU is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Active as Homoserine dehydrogenase, with EC number 1.1.1.3 Full crystallographic information is available from OCA.

Reference

Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases., DeLaBarre B, Thompson PR, Wright GD, Berghuis AM, Nat Struct Biol. 2000 Mar;7(3):238-44. PMID:10700284

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