Research Groups
Mammalian Biology: Structural and Computational Biology
Research Interests and Description
Staff Research Scientist: Arulandu Arockiasamy
Group Leader: Amit Sharma
Group Members
Research Interests
Membrane proteins, metal-ion transport, specialized protein secretion and Mycobacteria, Structural Biology.Description of Research
Structural Biology of Mycobacterial
membrane proteins
The Group's primary aim is to understand
the molecular mechanisms behind two vital biological processes such as
metal-ion and virulent protein translocation across inner membrane of
Mycobacteria, in particular Mycobacterium tuberculosis (M. tb). Mycobacterial genomes, in particular the
intracellular human pathogen M.tb, code for several metal-ion transporters. Experimental
data on metal-ion delivery, selection and import/export in M.tb is lacking. Hence,
a systematic in vitro approach is undertaken to study these putative transporters
for metal-ion preference and translocation using biochemical and structural
biological tools. We have devised a strategy to do parallel cloning and
expression to facilitate faster and efficient screening of as many as
transporters possible from M. tb in a shorter time to find candidates amenable
for structural and functional characterization. We expressed one of the
transporters using this strategy and work is in progress to adopt the method
for other transporters in the same family. We have also developed a
co-expression strategy to express protein-protein complexes of specialised
protein secretion machinery from M. tb in E. coli. In addition to integral
membrane proteins, we work on surface attached proteins of Mycobacteria like
PE_PGRS and a couple of interesting soluble proteins and protein-protein
complexes.
Publications
Xu, M., Arockiasamy, A., Struck, D.K., Swanson, S., Sacchettini, J.C., Young, R. 2005. Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science 307, 113-117
Arockiasamy, A., Murthy, G.S., Rukmini, M.R., Sundara Baalaji, N., Katpally, U.C., Krishnaswamy, S. 2004. Conformational epitope mapping of OmpC, a major cell surface antigen from S. typhi. J. Struct. Biol. 148, 22-33
Arockiasamy, A.Kumar, P.D., Sundara Baalaji, N., Rukmini, M.R., Krishnaswamy, S. 2004. Folding and structural stability of OmpC from Salmonella typhi: Role of LPS and environment. Curr. Sci. 87, 197-202
