1azy
From Proteopedia
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STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Overview
Two new crystal forms of Escherichia coli thymidine phosphorylase (EC, 2.4.2.4) have been found; a monoclinic form (space group P21) and an, orthorhombic form (space group I222). These structures have been solved, and compared to the previously determined tetragonal form (space group, P43212). This comparison provides evidence of domain movement of the alpha, (residues 1 to 65, 163 to 193) and alpha/beta (residues 80 to 154, 197 to, 440) domains, which is thought to be critical for enzymatic activity by, closing the active site cleft. Three hinge regions apparently allow the, alpha and alpha/beta-domains to move relative to each other. The, monoclinic model is the most open of the three models while the tetragonal, model is the most closed. Phosphate binding induces formation of a, ... [(full description)]
About this Structure
1AZY is a [Single protein] structure of sequence from [Escherichia coli]. Active as [Thymidine phosphorylase], with EC number [2.4.2.4]. Structure known Active Sites: P4A, P4B, TYA and TYB. Full crystallographic information is available from [OCA].
Reference
Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase., Pugmire MJ, Cook WJ, Jasanoff A, Walter MR, Ealick SE, J Mol Biol. 1998 Aug 14;281(2):285-99. PMID:9698549
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