3qy9

The Crystal Structure of Dihydrodipicolinate reductase from Staphylococcus aureus

spinqualitylabelsall models 3qy9, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qy9 is a 4 chain structure with sequence from Staphylococcus aureus subsp. aureus COL. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: ACT, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DAPB_STAAC Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.[HAMAP-Rule:MF_00102] Publication Abstract from PubMed 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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: DHDPRbindstoDHDPR by molecular sieving(View interaction). DHDPRbindstoDHDPR by dynamic light scattering(View interaction). DHDPRbindstoDHDPR by X-ray crystallography(View interaction). Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB).,Girish TS, Navratna V, Gopal B FEBS Lett. 2011 Aug 19;585(16):2561-7. Epub 2011 Jul 26. PMID:21803042 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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