1o2b

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Revision as of 20:38, 20 November 2007

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spinqualitylabelsall models 1o2b, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and PO4 at 2.45 A resolution

Overview

Like thymidylate synthase (TS) in eukaryotes, the thymidylate, synthase-complementing proteins (TSCPs) are mandatory for cell survival of, many prokaryotes in the absence of external sources of thymidylate., Details of the mechanism of this novel family of enzymes are unknown., Here, we report the structural and functional analysis of a TSCP from, Thermotoga maritima and its complexes with substrate, analogs, and, cofactor. The structures presented here provide a basis for rationalizing, the TSCP catalysis and reveal the possibility of the design of an, inhibitor. We have identified a new helix-loop-strand FAD binding motif, characteristic of the enzymes in the TSCP family. The presence of a, hydrophobic core with residues conserved among the TSCP family suggests a, common overall fold.

About this Structure

1O2B is a Single protein structure of sequence from Thermotoga maritima with PO4 and FAD as ligands. Full crystallographic information is available from OCA.

Reference

Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein., Mathews II, Deacon AM, Canaves JM, McMullan D, Lesley SA, Agarwalla S, Kuhn P, Structure. 2003 Jun;11(6):677-90. PMID:12791256

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