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2w6r
From Proteopedia
Revision as of 02:00, 1 October 2014 by OCA (Talk | contribs)
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Hocker B, Lochner A, Seitz T, Claren J, Sterner R. High-Resolution Crystal Structure of an Artificial (betaalpha)(8)-Barrel Protein Designed from Identical Half-Barrels (dagger) (double dagger). Biochemistry. 2009 Jan 23. PMID:19166324 doi:10.1021/bi802125b
