Journal article
Structure and Function of N-Acetylmannosamine Kinases from Pathogenic Bacteria
Thanuja Gangi Setty, Arunabha Sarkar, David Coombes, Renwick CJ Dobson, Ramaswamy Subramanian
ACS Omega | AMER CHEMICAL SOC | Published : 2020
Abstract
Several pathogenic bacteria import and catabolize sialic acids as a source of carbon and nitrogen. Within the sialic acid catabolic pathway, the enzyme N-acetylmannosamine kinase (NanK) catalyzes the phosphorylation of N-acetylmannosamine to N-acetylmannosamine-6-phosphate. This kinase belongs to the ROK superfamily of enzymes, which generally contain a conserved zinc-finger (ZnF) motif that is important for their structure and function. Previous structural studies have shown that the ZnF motif is absent in NanK of Fusobacterium nucleatum (Fn-NanK), a Gram-negative bacterium that causes the gum disease gingivitis. However, the effect in loss of the ZnF motif on the kinase activity is unknown..
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Awarded by Department of Biotechnology
Awarded by DBT-Indo Swedish grant
Awarded by DBT-B-life grant
Awarded by NCBS X-ray facility grant
Funding Acknowledgements
We thank the ESRF Access Program of RCB (supported by Department of Biotechnology grant BT/INF/22/SP22660/2017). We thank SOLEIL Synchrotron (Proxima 1 beamline) and ESRF (ID29 beamline) for providing the beamtime for data collection. This research was supported by DBT-Indo Swedish grant (BT/IN/SWEDEN/41/SR/2013), DBT-B-life grant (BT/PR5081/INF/156/2012), NCBS X-ray facility grant (BT/PR12422/MED/31/287/214), and a grant from the DST for SR. We thank Nitish Sathyanarayana, Dr. Swagatha Ghosh, and Dr. Rhawnie Caing-Carlsson for their contributions toward the initial stages of the work; Dr. Chetan Arya for the help with the ChemDraw figures of the sialic acid pathway; and Dr. Sanchari Banerjee for critical reading of the manuscript. T.G.S. would like to acknowledge senior research fellowship support from the Council of Scientific and Industrial Research (CSIR).