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Disulfide engineering at the dimer interface of Lactobacillus casei thymidylate synthase: Crystal structure of the T155C/E188C/C244T mutant

Published online by Cambridge University Press:  01 April 1999

S.S. VELANKER ,
R.S. GOKHALE ,
SOUMYA S. RAY ,
B. GOPAL ,
S. PARTHASARATHY ,
D.V. SANTI ,
P. BALARAM  and
M.R.N. MURTHY
S.S. VELANKER
Affiliation:
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
R.S. GOKHALE
Affiliation:
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
SOUMYA S. RAY
Affiliation:
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
B. GOPAL
Affiliation:
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
S. PARTHASARATHY
Affiliation:
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
D.V. SANTI
Affiliation:
Department of Biochemistry & Biophysics, University of California, San Francisco, California 94143
P. BALARAM
Affiliation:
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India Chemical Biology Unit, Jawaharlal Nehru Center for Advanced Scientific Research, Bangalore 560 012, India
M.R.N. MURTHY
Affiliation:
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
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Abstract

The crystal structure of a covalently cross-linked Lactobacillus casei thymidylate synthase has been determined at 2.8 Å resolution. The sites for mutation to achieve the bis-disulfide linked dimer were identified using the disulfide modeling program MODIP. The mutant so obtained was found to be remarkably thermostable. This increase in stability has been reasoned to be entirely a consequence of the covalent gluing between the two subunits.

Keywords

dimer interfacedisulfide engineeringstabilitythymidylate synthase

Information

Type
FOR THE RECORD
Information
Protein Science , Volume 8 , Issue 4 , April 1999 , pp. 930 - 933
Copyright
© 1999 The Protein Society

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