1ukk

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Revision as of 02:00, 25 November 2007

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spinqualitylabelsall models 1ukk, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of Osmotically Inducible Protein C from Thermus thermophilus

Overview

The X-ray crystallographic structure of osmotically inducible Protein C, from the thermophilic bacterium, Thermus thermophilus HB8, was solved to, 1.6A using the multiple wavelength anomalous dispersion method and a, selenomethionine incorporated protein (Se-MAD). The crystal space group, was P1 with cell dimensions of a=37.58 A, b=40.95 A, c=48.14 A, alpha=76.9, degrees, beta=74.0 degrees and gamma=64.1 degrees. The two tightly, interacting monomers in the asymmetric unit are related by a, non-crystallographic 2-fold. The dimer structure is defined primarily by, two very long anti-parallel, over-lapping alpha-helices at the core, with, a further six-stranded anti-parallel beta-sheet on the outside of the, structure. With respect to the beta-sheets, both A and B monomers, contribute three strands each resulting in an intertwining of the, structure. The active site consists of two cysteine residues from one, monomer and an arginine and glutamic acid from the other. Enzymatic assays, have revealed that T.thermophilus OsmC has a hydroperoxide peroxidase, activity.

About this Structure

1UKK is a Single protein structure of sequence from Thermus thermophilus with TRS as ligand. Full crystallographic information is available from OCA.

Reference

Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C., Rehse PH, Ohshima N, Nodake Y, Tahirov TH, J Mol Biol. 2004 May 14;338(5):959-68. PMID:15111059

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