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Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB)

Girish, Tavarekere S and Navratna, Vikas and Gopal, B (2011) Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB). In: FEBS Letters, 585 (16). pp. 2561-2567.

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Official URL: http://dx.doi.org/10.1016/j.febslet.2011.07.021


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: DHDPR binds to DHDPR by molecular sieving (View interaction). DHDPR binds to DHDPR by dynamic light scattering (View interaction). DHDPR binds to DHDPR by X-ray crystallography (View interaction). (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science B.V.
Keywords: DHDPR;DapB;MRSA;Lysine/m-Dap biosynthesis
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: Id for Latest eprints
Date Deposited: 03 Sep 2011 10:24
Last Modified: 03 Sep 2011 10:24
URI: http://eprints.iisc.ac.in/id/eprint/40407

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