3QY9
The Crystal Structure of Dihydrodipicolinate reductase from Staphylococcus aureus
Summary for 3QY9
| Entry DOI | 10.2210/pdb3qy9/pdb |
| Descriptor | Dihydrodipicolinate reductase, SULFATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | rossmann fold, reductase, nadh, nadph, dihydrodipicolinate, oxidoreductase |
| Biological source | Staphylococcus aureus |
| Cellular location | Cytoplasm (By similarity): Q5HG24 |
| Total number of polymer chains | 4 |
| Total formula weight | 110317.94 |
| Authors | Girish, T.S.,Gopal, B. (deposition date: 2011-03-03, release date: 2011-08-03, Last modification date: 2023-11-01) |
| Primary citation | Girish, T.S.,Navratna, V.,Gopal, B. Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB) Febs Lett., 585:2561-2567, 2011 Cited by PubMed Abstract: Lysine biosynthesis proceeds by the nucleotide-dependent reduction of dihydrodipicolinate (DHDP) to tetrahydrodipicolinate (THDP) by dihydrodipicolinate reductase (DHDPR). The S. aureus DHDPR structure reveals different conformational states of this enzyme even in the absence of a substrate or nucleotide-cofactor. Despite lacking a conserved basic residue essential for NADPH interaction, S. aureus DHDPR differs from other homologues as NADPH is a more preferred co-factor than NADH. The structure provides a rationale-Lys35 compensates for the co-factor site mutation. These observations are significant for bi-ligand inhibitor design that relies on ligand-induced conformational changes as well as co-factor specificity for this important drug target. PubMed: 21803042DOI: 10.1016/j.febslet.2011.07.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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