1ukk
From Proteopedia
|
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 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
Page seeded by OCA on Thu Feb 21 15:25:31 2008
Categories: Single protein | Thermus thermophilus | Kuramitsu, S. | Miyano, M. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Rehse, P H. | Tahirov, T H. | Yokoyama, S. | TRS | Cysteinesulfinic acid | Inducible | Osmotic | Peroxidase | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
