Journal article
Cloning, expression, purification, crystallization and preliminary X-ray diffraction studies of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus
RA North, SA Kessans, SC Atkinson, H Suzuki, AJA Watson, BR Burgess, LM Angley, AO Hudson, A Varsani, MDW Griffin, AJ Fairbanks, RCJ Dobson
Acta Crystallographica Section F Structural Biology and Crystallization Communications | INT UNION CRYSTALLOGRAPHY | Published : 2013
Abstract
The enzyme N-acetylneuraminate lyase (EC 4.1.3.3) is involved in the metabolism of sialic acids. Specifically, the enzyme catalyzes the retro-aldol cleavage of N-acetylneuraminic acid to form N-acetyl-d-mannosamine and pyruvate. Sialic acids comprise a large family of nine-carbon amino sugars, all of which are derived from the parent compound N-acetylneuraminic acid. In recent years, N-acetylneuraminate lyase has received considerable attention from both mechanistic and structural viewpoints and has been recognized as a potential antimicrobial drug target. The N-acetylneuraminate lyase gene was cloned from methicillin-resistant Staphylococcus aureus genomic DNA, and recombinant protein was e..
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Awarded by New Zealand Royal Society Marsden Fund
Awarded by US Army Research Office
Awarded by United States National Science Foundation (NSF)
Awarded by Australian Research Council
Funding Acknowledgements
We acknowledge the support and assistance of the friendly staff at the CSIRO-Collaborative Crystallization Centre at CSIRO Material Science and Engineering, Parkville, Melbourne and the MX beamline scientists at the Australian Synchrotron, Victoria, Australia. Parts of this research were undertaken at the MX2 beamline of the Australian Synchrotron, Victoria, Australia. Travel to the Australian Synchrotron was supported by the New Zealand Synchrotron Group. RCJD acknowledges the C. R. Roper Bequest for Fellowship support, the New Zealand Royal Society Marsden Fund for funding support, in part (contract UOC1013), and the US Army Research Laboratory and US Army Research Office under contract/grant No. W911NF-11-1-0481 for support, in part. HS acknowledges FY 2012 Researcher Exchange Program between the Japan Society for the Promotion of Science and the Royal Society of New Zealand for salary support. AOH acknowledges the United States National Science Foundation (NSF) award No. MCB-1120541. MDWG is the recipient of an Australian Research Council Post Doctoral Fellowship (project No. DP110103528). We especially thank Jackie Healy for her magnanimous technical support.