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

S. S. Velanker; R. S. Gokhale; Soumya S. Ray; B. Gopal; S. Parthasarathy; D. V. Santi; P. Balaram; M. R.N. Murthy

doi:10.1110/ps.8.4.930

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

S. S. Velanker, R. S. Gokhale, Soumya S. Ray, B. Gopal, S. Parthasarathy, D. V. Santi, P. Balaram, M. R.N. Murthy

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

The crystal structure of a covalently cross-linked Lactobacillus casei thymidylate synthase has been determined at 2.8 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.

Original language	English (US)
Pages (from-to)	930-933
Number of pages	4
Journal	Protein Science
Volume	8
Issue number	4
DOIs	https://doi.org/10.1110/ps.8.4.930
State	Published - 1999
Externally published	Yes

Keywords

Dimer interface
Disulfide engineering
Stability
Thymidylate synthase

ASJC Scopus subject areas

Biochemistry
Molecular Biology

Access to Document

10.1110/ps.8.4.930

Cite this

@article{471058b0e5e94b399d613f1ddd1e7729,

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

abstract = "The crystal structure of a covalently cross-linked Lactobacillus casei thymidylate synthase has been determined at 2.8 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 interface, Disulfide engineering, Stability, Thymidylate synthase",

author = "Velanker, {S. S.} and Gokhale, {R. S.} and Ray, {Soumya S.} and B. Gopal and S. Parthasarathy and Santi, {D. V.} and P. Balaram and Murthy, {M. R.N.}",

year = "1999",

doi = "10.1110/ps.8.4.930",

language = "English (US)",

volume = "8",

pages = "930--933",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Cold Spring Harbor Laboratory Press",

number = "4",

}

TY - JOUR

T1 - Disulfide engineering at the dimer interface of Lactobacillus casei thymidylate synthase

T2 - Crystal structure of the T155C/E188C/C244T mutant

AU - Velanker, S. S.

AU - Gokhale, R. S.

AU - Ray, Soumya S.

AU - Gopal, B.

AU - Parthasarathy, S.

AU - Santi, D. V.

AU - Balaram, P.

AU - Murthy, M. R.N.

PY - 1999

Y1 - 1999

N2 - The crystal structure of a covalently cross-linked Lactobacillus casei thymidylate synthase has been determined at 2.8 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.

AB - The crystal structure of a covalently cross-linked Lactobacillus casei thymidylate synthase has been determined at 2.8 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.

KW - Dimer interface

KW - Disulfide engineering

KW - Stability

KW - Thymidylate synthase

UR - http://www.scopus.com/inward/record.url?scp=0032891249&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032891249&partnerID=8YFLogxK

U2 - 10.1110/ps.8.4.930

DO - 10.1110/ps.8.4.930

M3 - Article

C2 - 10211840

AN - SCOPUS:0032891249

SN - 0961-8368

VL - 8

SP - 930

EP - 933

JO - Protein Science

JF - Protein Science

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this