1odk

From Proteopedia

Revision as of 11:30, 30 October 2007

PURINE NUCLEOSIDE PHOSPHORYLASE FROM THERMUS THERMOPHILUS

Overview

The purine nucleoside phosphorylase from Thermus thermophilus crystallized, in space group P4(3)2(1)2 with the unit cell dimensions a = 131.9 A and c, = 169.9 A and one biologically active hexamer in the asymmetric unit. The, structure was solved by the molecular replacement method and refined at a, 1.9A resolution to an r(free) value of 20.8%. The crystals of the binary, complex with sulfate ion and ternary complexes with sulfate and adenosine, or guanosine were also prepared and their crystal structures were refined, at 2.1A, 2.4A and 2.4A, respectively. The overall structure of the, T.thermophilus enzyme is similar to the structures of hexameric enzymes, from Escherichia coli and Sulfolobus solfataricus, but significant, differences are observed in the purine base recognition site. A ... [(full description)]

About this Structure

1ODK is a [Single protein] structure of sequence from [Thermus thermophilus] with GOL as [ligand]. Active as [S-methyl-5-thioadenosine phosphorylase], with EC number [2.4.2.28]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of purine nucleoside phosphorylase from Thermus thermophilus., Tahirov TH, Inagaki E, Ohshima N, Kitao T, Kuroishi C, Ukita Y, Takio K, Kobayashi M, Kuramitsu S, Yokoyama S, Miyano M, J Mol Biol. 2004 Apr 9;337(5):1149-60. PMID:15046984

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