1tls
From Proteopedia
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THYMIDYLATE SYNTHASE TERNARY COMPLEX WITH FDUMP AND METHYLENETETRAHYDROFOLATE
Overview
Two crystal structures for E. coli thymidylate synthase (TS) bound to the, mechanism-based inhibitor 5-fluoro-dUMP (FdUMP) and, methylenetetrahydrofolate (CH2THF) have been determined to 2.6 and 2.2 A, nominal resolutions, with crystallographic R factors of 0.180 and 0.178, respectively. The inhibitor and cofactor are well ordered in both, structures and display covalent links to each other and to Cys 146 in the, TS active site. The structures are in general agreement with a previous, report for this complex (D. A. Matthews et al. (1990) J. Mol. Biol. 214, 937-948), but differ in two key respects: (i) the methylene bridge linking, FdUMP and CH2THF is rotated about 60 degrees to a different position and, (ii) the electron density for C6 of FdUMP, which is covalently linked to, Cys 146, is ... [(full description)]
About this Structure
1TLS is a [Single protein] structure of sequence from [Escherichia coli] with UFP and C2F as [ligands]. Active as [[1]], with EC number [2.1.1.45]. Full crystallographic information is available from [OCA].
Reference
Use of strain in a stereospecific catalytic mechanism: crystal structures of Escherichia coli thymidylate synthase bound to FdUMP and methylenetetrahydrofolate., Hyatt DC, Maley F, Montfort WR, Biochemistry. 1997 Apr 15;36(15):4585-94. PMID:9109668
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