1clk

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1clk, resolution 1.90Å

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CRYSTAL STRUCTURE OF STREPTOMYCES DIASTATICUS NO.7 STRAIN M1033 XYLOSE ISOMERASE AT 1.9 A RESOLUTION WITH PSEUDO-I222 SPACE GROUP

Overview

The structure of xylose isomerase (XyI) from Streptomyces diastaticus No., 7 strain M1033 (SDXyI) has been refined at 1.85 A resolution to, conventional and free R factors of 0.166 and 0.219, respectively. SDXyI, was crystallized in space group P2(1)2(1)2, with unit-cell parameters a =, 87.976, b = 98.836, c = 93.927 A. One dimer of the tetrametric molecule is, found in each asymmetric unit. Each monomer consists of two domains: a, large N-terminal domain (residues 1-320), containing a parallel, eight-stranded alpha/beta barrel, and a small C-terminal loop (residues, 321-387), containing five helices linked by random coil. The four monomers, are essentially identical in the tetramer, possessing non-crystallographic, 222 symmetry with one twofold axis essentially coincident with the, crystallographic twofold axis in the space group P2(1)2(1)2, which may, explain why the diffraction pattern has strong pseudo-I222 symmetry even, at medium resolution. The crystal structures of XyIs from different, bacterial strains, especially from Streptomyces, are similar. The alpha2, helix of the alpha/beta barrel has a different position in the structures, of different XyIs. The conformation of C-terminal fragment 357-364 in the, SDXyI structure has a small number of differences to that of other XyIs., Two Co(2+) ions rather than Mg(2+) ions exist in the active site of the, SDXyI structure; SDXyI seems to prefer to bind Co(2+) ions rather than, Mg(2+) ions.

About this Structure

1CLK is a Single protein structure of sequence from Streptomyces diastaticus with MG and CO as ligands. Active as Xylose isomerase, with EC number 5.3.1.5 Full crystallographic information is available from OCA.

Reference

Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution., Zhu X, Teng M, Niu L, Xu C, Wang Y, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):129-36. PMID:10666592

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