Structural highlights
FunctionPublication Abstract from PubMedThe 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 2.40 A resolution. The structure reveals a high level of structural homology to the sterol carrier protein (SCP) family, suggesting a potential role of MSMEG_5817 in the binding and transportation of biologically relevant lipids required for bacterial survival. The lipid-binding capacity of MSMEG_5817 was confirmed by ELISA, revealing binding to a number of phospholipids with varying binding specificities compared with Homo sapiens SCP. A potential lipid-binding site was probed by alanine-scanning mutagenesis, revealing structurally relevant residues and a binding mechanism potentially differing from that of the SCPs. A structural and functional investigation of a novel protein from Mycobacterium smegmatis implicated in mycobacterial macrophage survivability.,Shahine A, Littler D, Brammananath R, Chan PY, Crellin PK, Coppel RL, Rossjohn J, Beddoe T Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2264-76. doi:, 10.1107/S139900471401092X. Epub 2014 Aug 23. PMID:25195741[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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