2w6r | pdb_00002w6r

CRYSTAL STRUCTURE OF AN ARTIFICIAL (BA)8-BARREL PROTEIN DESIGNED FROM IDENTICAL HALF BARRELS

spinqualitylabelsall models 2w6r, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w6r is a 1 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2a0n, 1thf, 1gpw, 1vh7 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Ample evidence suggests that the ubiquitous (betaalpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of an ancestral (betaalpha)(4)-half-barrel. To reconstruct this process in the laboratory with a model protein, we earlier fused two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF) and stepwise stabilized the resulting HisF-CC construct. We now further increased its stability and solubility by introducing two additional amino acid exchanges, which allowed us to crystallize the resulting artificial (betaalpha)(8)-barrel protein HisF-C***C. The analysis of its X-ray structure at 2.1 A resolution reveals a striking similarity to wild-type HisF, helps us to understand its improved stability, and provides further insights into the evolution of (betaalpha)(8)-barrel proteins. High-Resolution Crystal Structure of an Artificial (betaalpha)(8)-Barrel Protein Designed from Identical Half-Barrels (dagger) (double dagger).,Hocker B, Lochner A, Seitz T, Claren J, Sterner R Biochemistry. 2009 Jan 23. PMID:19166324 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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