Journal article
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of N-acetylmannosamine-6-phosphate 2-epimerase from methicillin-resistant Staphylococcus aureus
RA North, SA Kessans, MDW Griffin, AJA Watson, AJ Fairbanks, RCJ Dobson
Acta Crystallographica Section F Structural Biology Communications | INT UNION CRYSTALLOGRAPHY | Published : 2014
Abstract
Sialic acids are one of the most important carbohydrate classes in biology. Some bacterial pathogens can scavenge sialic acids from their surrounding environment and degrade them as a source of carbon, nitrogen and energy. This sequestration and subsequent catabolism of sialic acid require a cluster of genes known as the 'Nan-Nag' cluster. The enzymes coded by these genes are important for pathogen colonization and persistence. Importantly, the Nan-Nag genes have proven to be essential for Staphylococcus aureus growth on sialic acids, suggesting that the pathway is a viable antibiotic drug target. The enzyme N-acetylmannosamine-6-phosphate 2-epimerase is involved in the catabolism of sialic ..
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Awarded by Ministry of Business, Innovation and Employment
Awarded by New Zealand Royal Society Marsden Fund
Awarded by US Army Research Office
Awarded by New Zealand Ministry of Business, Innovation & Employment (MBIE)
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. Travel to the Australian Synchrotron was supported by the New Zealand Synchrotron Group. RCJD acknowledges the following for funding support, in part: (i) the Ministry of Business, Innovation and Employment (contract UOCX1208); (ii) the New Zealand Royal Society Marsden Fund (contract UOC1013); and (iii) the US Army Research Laboratory and US Army Research Office under contract/grant No. W911NF-11-1-0481. We especially thank Jackie Healy for her steely technical support.