Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of thymidylate kinase (TTHA1607) from Thermus thermophilus HB8

Chaudhary, Santosh Kumar and Jeyakanthan, Jeyaraman and Sekar, Kanagaraj (2013) Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of thymidylate kinase (TTHA1607) from Thermus thermophilus HB8. In: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 69 (Part 2). pp. 118-121.

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Abstract

Nucleotide biosynthesis plays a key role in cell survival and cell proliferation. Thymidylate kinase is an enzyme that catalyses the conversion of dTMP to dTDP using ATP-Mg2+ as a phosphoryl-donor group. This enzyme is present at the junction of the de novo and salvage pathways; thus, any inhibitor designed against it will result in cell death. This highlights the importance of this enzyme as a drug target. Thymidylate kinase from the extremely thermophilic organism Thermus thermophilus HB8 has been expressed, purified and crystallized using the microbatch method. The crystals diffracted to a resolution of 1.83 angstrom and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 39.50, b = 80.29, c = 122.55 angstrom. Preliminary studies revealed the presence of a dimer in the asymmetric unit with a Matthews coefficient (V-M) of 2.18 angstrom(3) Da(-1).

Item Type:	Journal Article
Publication:	ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Publisher:	WILEY-BLACKWELL
Additional Information:	Copyright for this article belongs to WILEY-BLACKWELL, HOBOKEN, USA
Department/Centre:	Division of Interdisciplinary Sciences > Supercomputer Education & Research Centre Division of Physical & Mathematical Sciences > Physics
Date Deposited:	06 Mar 2013 11:09
Last Modified:	06 Mar 2013 11:09
URI:	http://eprints.iisc.ac.in/id/eprint/45941

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