3qy9

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.