1ebu

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[[Image:1ebu.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1ebu| PDB=1ebu | SCENE= }}
{{STRUCTURE_1ebu| PDB=1ebu | SCENE= }}
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'''HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE'''
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===HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 10700284 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10700284}}
==About this Structure==
==About this Structure==
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[[Category: Homoserine]]
[[Category: Homoserine]]
[[Category: Ternary]]
[[Category: Ternary]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:28:07 2008''

Revision as of 21:28, 30 June 2008

Image:1ebu.png

Template:STRUCTURE 1ebu

HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE

Template:ABSTRACT PUBMED 10700284

About this Structure

1EBU is a Single protein structure of sequence from Saccharomyces cerevisiae. 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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