Format

Send to

Choose Destination
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt 7):659-61. doi: 10.1107/S1744309108016746. Epub 2008 Jun 28.

Purification, crystallization and preliminary X-ray diffraction studies to near-atomic resolution of dihydrodipicolinate synthase from methicillin-resistant Staphylococcus aureus.

Author information

1
Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria 3010, Australia.

Abstract

In recent years, dihydrodipicolinate synthase (DHDPS; EC 4.2.1.52) has received considerable attention from both mechanistic and structural viewpoints. DHDPS is part of the diaminopimelate pathway leading to lysine, coupling (S)-aspartate-beta-semialdehyde with pyruvate via a Schiff base to a conserved active-site lysine. In this paper, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DHDPS from methicillin-resistant Staphylococcus aureus, an important bacterial pathogen, are reported. The enzyme was crystallized in a number of forms, predominantly from PEG precipitants, with the best crystal diffracting to beyond 1.45 A resolution. The space group was P1 and the unit-cell parameters were a = 65.4, b = 67.6, c = 78.0 A, alpha = 90.1, beta = 68.9, gamma = 72.3 degrees . The crystal volume per protein weight (V(M)) was 2.34 A(3) Da(-1), with an estimated solvent content of 47% for four monomers per asymmetric unit. The structure of the enzyme will help to guide the design of novel therapeutics against the methicillin-resistant S. aureus pathogen.

PMID:
18607102
PMCID:
PMC2443978
DOI:
10.1107/S1744309108016746
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for International Union of Crystallography Icon for PubMed Central
Loading ...
Support Center