1tis
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(New page: 200px<br /><applet load="1tis" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tis, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 01:11, 21 November 2007
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CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE FROM T4 PHAGE
Overview
Thymidylate synthase from phage T4 (T4TS) is part of a complex of several, enzymes required for coordinate DNA synthesis in infected Escherichia coli, cells. It has been proposed that similar complexes of enzymes related to, DNA synthesis are also functional in eukaryotes [Pardee, A. B. (1989), Science 246, 603-608]. To delineate the role of structure in the function, of this complex, we have solved the structure of T4TS as a basis for, mapping the complex by mutagenesis. The 3.1 A structure of the unliganded, enzyme was determined by molecular replacement and refined to 19.9% for, all data. Three inserts and one deletion in the coding region are unique, to T4TS, and all sites lie on one side of the enzyme surface, possibly, encoding unique T4 specific intermolecular interactions during the, infective cycle. The crystal structure is generally in the open, unliganded conformation seen in unliganded E. coli TS, as opposed to the, closed, ternary complex conformation, except that the critically important, C-terminus is inserted into the active site hydrogen bonded to residue, Asn85, as seen in functional ternary complex structures. Other differences, between E. coli TS and T4TS appear to explain the enhanced binding of, folyl polyglutamate to the latter.
About this Structure
1TIS is a Single protein structure of sequence from Bacteriophage t4 with PO4 as ligand. Active as Thymidylate synthase, with EC number 2.1.1.45 Full crystallographic information is available from OCA.
Reference
Crystal structure of thymidylate synthase from T4 phage: component of a deoxynucleoside triphosphate-synthesizing complex., Finer-Moore JS, Maley GF, Maley F, Montfort WR, Stroud RM, Biochemistry. 1994 Dec 27;33(51):15459-68. PMID:7803410
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