4NSS

A structural and functional investigation of a novel protein from Mycobacterium smegmatis implicated in mycobacterial macrophage survivability

Summary for 4NSS

• Entry DOI: 10.2210/pdb4nss/pdb
• Descriptor: Mycobacterial protein, GLYCEROL (3 entities in total)
• Functional Keywords: mycobacterial survival, unknown function
• Biological source: Mycobacterium smegmatis
• Total number of polymer chains: 2
• Total formula weight: 31521.71

Authors

Shahine, A.E.,Littler, D.,Brammananath, R.,Chan, P.Y.,Crellin, P.K.,Coppel, R.L.,Rossjohn, J.,Beddoe, T. (deposition date: 2013-11-28, release date: 2014-09-10, Last modification date: 2024-02-28)

Primary citation

Shahine, A.,Littler, D.,Brammananath, R.,Chan, P.Y.,Crellin, P.K.,Coppel, R.L.,Rossjohn, J.,Beddoe, T.
A structural and functional investigation of a novel protein from Mycobacterium smegmatis implicated in mycobacterial macrophage survivability.
Acta Crystallogr.,Sect.D, 70:2264-2276, 2014

PubMed 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 2.40 Å 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.

PubMed: 25195741
DOI: 10.1107/S139900471401092X

Experimental method

X-RAY DIFFRACTION (2.4 Å)