3tms
From Proteopedia
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PLASTIC ADAPTATION TOWARD MUTATIONS IN PROTEINS: STRUCTURAL COMPARISON OF THYMIDYLATE SYNTHASES
Overview
The structure of thymidylate synthase (TS) from Escherichia coli was, solved from cubic crystals with a = 133 A grown under reducing conditions, at pH 7.0, and refined to R = 22% at 2.1 A resolution. The structure is, compared with that from Lactobacillus casei solved to R = 21% at 2.3 A, resolution. The structures are compared using a difference distance, matrix, which identifies a common core of residues that retains the same, relationship to one another in both species. After subtraction of the, effects of a 50 amino acid insert present in Lactobacillus casei, differences in position of atoms correlate with temperature factors and, with distance from the nearest substituted residue. The dependence of, structural difference on thermal factor is parameterized and reflects both, errors in coordinates that correlate with thermal factor, and the, increased width of the energy well in which atoms of high thermal factor, lie. The dependence of structural difference on distance from the nearest, substitution also depends on thermal factors and shows an exponential, dependence with half maximal effect at 3.0 A from the substitution. This, represents the plastic accommodation of the protein which is parameterized, in terms of thermal B factor and distance from a mutational change.
About this Structure
3TMS is a Single protein structure of sequence from Escherichia coli with PO4 as ligand. Active as Thymidylate synthase, with EC number 2.1.1.45 Full crystallographic information is available from OCA.
Reference
Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases., Perry KM, Fauman EB, Finer-Moore JS, Montfort WR, Maley GF, Maley F, Stroud RM, Proteins. 1990;8(4):315-33. PMID:2128651
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