S. Eswaramoorthy is a scientist in the Structural Genomics Group at the BNL Biology Department which is a partner
in the New York Structural Genomics Research Consortium. The NYSGRC is a collaboratory of the Albert Einstein College
of Medicine, BNL, Columbia University, Structural Genomics Inc., The Rockefeller University, University of California
at San Francisco, and the Sloan Kettering Institute. The BNL Biology group is advancing the efficient crystallographic
structure determination of NYSGRC targeted proteins, and currently includes the following scientists and post doctoral
fellows: S. Swaminathan (Principal Investigator), S. Eswaramoorthy, D. Kumaran, R. Agarwal, S. Jayaraman, N. Krishnamurthy, and J-S. Jiang.
Our interests are to understand the function of selected proteins such as toxins
and amino-acid processing enzymes through crystallographic structure analysis.
The plant toxin ricin has been known for decades and its catalytic activity is
studied well. Generally, the functional mechanism of toxins involves cell binding,
internalization, and catalytic activity. Internalization or cell permeation is
the part that needs more understanding and will yield many useful results. Our
effort is to study the cell binding and internalization of ricin toxin through
crystal structure analysis of ricin B chain - peptide/oligosaccharide complexes.
The peptides that have high binding affinity to the toxin are selected from
phage display libraries. The results from study are a prerequisite for toxin
detection and vaccine development.
Glutamine is one of the most abundant amino acids in the body and is found in
all tissues. The metabolism of glutamine requires the enzyme, glutaminase.
Glutaminase hydrolyzes the amide nitrogen of glutamine and produces glutamate
and an ammonium ion. We are studying by crystallographic methods the structure
function relationships of glutaminase.
Kumaran, D., Eswaramoorthy S., Furey, W., Navaza, J., Sax, M., and Swaminathan S.
Domain organization in Clostridium botulinum neurotoxin type E is unique: Its implication in faster translocation.
Journal of Molecular Biology, 386(1):233-245 (February, 2009).
Madegowda M., Eswaramoorthy S., Burley S.K. and Swaminathan S.
X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus.
PROTEINS: Structure, Function, and Bioinformatics, 71(2):534-540 (2008).
Tyagi R., Eswaramoorthy S., Burley S.K., Raushel F.M. and Swaminathan S.
A common catalytic mechanism for proteins of HutI family.
Biochemistry, 47(20):5608-5615 (2008).
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V.,
Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D.,
Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A.,
Faber-Barata J., Chance M.R., Sali A., Fiser A., Zhang Z.Y., Lawrence D.S. and Burley S. K.
Structural genomics of protein phosphatases.
Journal of Structural and Functional Genomics, 8(2-3):121-140 (2007).
Eswaramoorthy S., Bonanno J.B., Burley S.K. and Swaminathan S.
Mechanism of action of a flavin-containing monooxygenase.
Proceedings of the National Academy of Sciences USA, 103(26):9832-9837 (2006).
Jayaraman S., Eswaramoorthy S., Ahmed S.A., Smith L.A. and Swaminathan S.
N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B.
Biochem Biophys Res Commun., 330(1):97-103 (2005).
Jayaraman S., Eswaramoorthy S., Kumaran D. and Swaminathan S.
Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin.
PROTEINS: Structure, Function, and Bioinformatics, 61(2):288-295 (2005).
Kumaran D., Eswaramoorthy S., Studier F.W. and Swaminathan S.
Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase), a ubiquitous cellular
Protein Sci., 14(3):719-726 (2005).
Agarwal R., Eswaramoorthy S., Kumaran D., Dunn J.J. and Swaminathan S.
Cloning, high level expression, purification, and crystallization of the full length Clostridium
botulinum neurotoxin type E light chain.
Protein Expr Purif., 34(1):95-102 (2004).
Agarwal R., Eswaramoorthy S., Kumaran D., Binz T. and Swaminathan S.
Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln
reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway.
Biochemistry, 43(21):6637-6644 (2004).
Eswaramoorthy S., Kumaran D., Keller J. and Swaminathan S.
Role of Metals in the biological activity of Clostridium botulinum neurotoxins.
Biochemistry, 43(8):2209-2216 (2004).
Eswaramoorthy S., Rao S.T., Pan B. and Sundaralingam M.
Structure of the dodecamer r(GAUCACUUCGGU) with four 5'-overhang nucleotides.
Acta Cryst., D60(1):8-12 (2004).
Swaminathan S., Eswaramoorthy S. and Kumaran D.
Structure and enzymatic activity of botulinum neurotoxins.
Mov. Disord. Suppl., 8: S17-22 (2004).
Eswaramoorthy S., Gerchman S., Graziano V., Kycia H., Studier F.W. and Swaminathan S.
Structure of a yeast hypothetical protein selected by a structural genomics approach.
Acta Cryst., D59(1):127-135 (2003).
Kumaran D., Eswaramoorthy S., Gerchman S.E., Kycia H., Studier F.W. and Swaminathan S.
Crystal structure of a putative CN hydrolase from yeast.
Proteins, 52(2):283-291 (2003).
Eswaramoorthy S., Kumaran D. and Swaminathan S.
A novel mechanism for Clostridium botulinum neurotoxin inhibition.
Biochemistry, 41(31):9795-9802 (2002).
Eswaramoorthy S., Kumaran D. and Swaminathan S.
Crystallographic evidence for doxorubicin binding to the receptor-binding site in
Clostridium botulinum neurotoxin B.
Acta Cryst., D57(11): 1743-1746 (2001).
Kumaran D., Eswaramoorthy S., Furey W., Sax M. and Swaminathan S.
Structure of staphylococcal enterotoxin C2 at various pH levels.
Acta Cryst., D57(9):1270-1275 (2001).
Kumaran D., Eswaramoorthy S., Luft B.J., Koide S., Dunn J.J., Lawson C.L. and Swaminathan S.
Crystal structure of outer surface protein C (OspC) from the Lyme
disease spirochete, Borrelia burgdorferi.
EMBO J., 20(5):971-978 (2001).
Full Text (pdf)
Kumar P.R., Eswaramoorthy S., Vithayathil P.J.and Viswamitra M.A.
The tertiary structure at 1.59 A resolution and the proposed amino acid sequence
of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti bainier.
J. Mol. Biol., 295(3):581-593 (2000).
Swaminathan S. and Eswaramoorthy S.
Structural analysis of the catalytic and binding sites of Clostridium botulinum
Nat. Struct. Biol., 7(8):693-699 (2000).
Sekar K., Eswaramoorthy S., Jain M.K. and Sundaralingam M.
Crystal structure of the complex of bovine pancreatic phospholipase A2 with the
Biochemistry, 36(46):14186-14191 (1997).
Eswaramoorthy S., Vithayathil P.J. and Viswamitra M.A.
Crystallization and preliminary X-ray crystallographic studies of thermostable
xylanase crystals isolated from Paecilomyces varioti.
J. Mol. Biol., 243(4):806-808 (1994).