1EBU
HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE
Summary for 1EBU
| Entry DOI | 10.2210/pdb1ebu/pdb |
| Related | 1EBF |
| Descriptor | HOMOSERINE DEHYDROGENASE, SODIUM ION, 3-AMINOMETHYL-PYRIDINIUM-ADENINE-DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | homoserine, dehydrogenase, dinucleotide, ternary, analogue, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 154515.59 |
| Authors | DeLaBarre, B.,Thompson, P.R.,Wright, G.D.,Berghuis, A.M. (deposition date: 2000-01-24, release date: 2000-03-08, Last modification date: 2023-11-15) |
| Primary citation | DeLaBarre, B.,Thompson, P.R.,Wright, G.D.,Berghuis, A.M. Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases. Nat.Struct.Biol., 7:238-244, 2000 Cited by PubMed Abstract: 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. PubMed: 10700284DOI: 10.1038/73359 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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