Journal article
A structural and functional investigation of a novel protein from Mycobacterium smegmatis implicated in mycobacterial macrophage survivability
A Shahine, D Littler, R Brammananath, PY Chan, PK Crellin, RL Coppel, J Rossjohn, T Beddoe
Acta Crystallographica Section D Biological Crystallography | INT UNION CRYSTALLOGRAPHY | Published : 2014
Abstract
The success of pathogenic mycobacterial species is owing in part to their ability to parasitize the generally inhospitable phagosomal environment of host macrophages, utilizing a variety of strategies to avoid their antimycobacterial capabilities and thereby enabling their survival. A recently identified gene target in Mycobacterium smegmatis, highly conserved within Mycobacterium spp. and denoted MSMEG-5817, has been found to be important for bacterial survival within host macrophages. To gain insight into its function, the crystal structure of MSMEG-5817 has been solved to 2.40Å resolution. The structure reveals a high level of structural homology to the sterol carrier protein (SCP) family..
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Funding Acknowledgements
We thank the staff of the Australian Synchrotron and Monash Macromolecular Crystallization Facility for assistance with crystallization and X-ray data collection. This work was supported by the Australian Research Council (ARC) Centre of Excellence in Structural and Functional Microbial Genomics and the National Health and Medical Research Council of Australia. JR is an NHMRC Australia Fellow and TB is a Pfizer Australian Research Fellow.