2QRJ
Crystal Structure of Sulfate-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae
Summary for 2QRJ
Entry DOI | 10.2210/pdb2qrj/pdb |
Related | 2Q99 |
Descriptor | Saccharopine dehydrogenase, NAD+, L-lysine-forming, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | sulfate, rossmann fold, alpha-aminoadipate pathway, fungal lysine biosynthesis, acetylation, amino-acid biosynthesis, cytoplasm, nad, oxidoreductase |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Cytoplasm : P38998 |
Total number of polymer chains | 1 |
Total formula weight | 44381.11 |
Authors | Andi, B.,Xu, H.,Cook, P.F.,West, A.H. (deposition date: 2007-07-28, release date: 2007-10-30, Last modification date: 2024-10-09) |
Primary citation | Andi, B.,Xu, H.,Cook, P.F.,West, A.H. Crystal Structures of Ligand-Bound Saccharopine Dehydrogenase from Saccharomyces cerevisiae Biochemistry, 46:12512-12521, 2007 Cited by PubMed Abstract: Three structures of saccharopine dehydrogenase (l-lysine-forming) (SDH) have been determined in the presence of sulfate, adenosine monophosphate (AMP), and oxalylglycine (OxGly). In the sulfate-bound structure, a sulfate ion binds in a cleft between the two domains of SDH, occupies one of the substrate carboxylate binding sites, and results in partial closure of the active site of the enzyme due to a domain rotation of almost 12 degrees in comparison to the apoenzyme structure. In the second structure, AMP binds to the active site in an area where the NAD+ cofactor is expected to bind. All of the AMP moieties (adenine ring, ribose, and phosphate) interact with specific residues of the enzyme. In the OxGly-bound structure, carboxylates of OxGly interact with arginine residues representative of the manner in which substrate (alpha-ketoglutarate and saccharopine) may bind. The alpha-keto group of OxGly interacts with Lys77 and His96, which are candidates for acid-base catalysis. Analysis of ligand-enzyme interactions, comparative structural analysis, corroboration with kinetic data, and discussion of a ternary complex model are presented in this study. PubMed: 17939687DOI: 10.1021/bi701428m PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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