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Publication Abstract from PubMed

The crystal structure of the uncharacterized protein SO2946 from Shewanella oneidensis MR-1 was determined with single-wavelength anomalous diffraction (SAD) and refined to 2.0 A resolution. The SO2946 protein consists of a short helical N-terminal domain and a large C-terminal domain with the "jelly-roll" topology. The protein assembles into a propeller consisting of three C-terminal blades arranged around a central core formed by the N-terminal domains. The function of SO2946 could not be inferred from the sequence since the protein represents an orphan with no sequence homologs, but the protein's structure bears a fold similar to that of proteins containing carbohydrate-binding modules. Features such as fold conservation, the presence of a conserved groove and a metal binding region are indicative that SO2946 may be an enzyme and could be involved in binding carbohydrate molecules.

Structure of SO2946 orphan from Shewanella oneidensis shows "jelly-roll" fold with carbohydrate-binding module.,Nocek B, Bigelow L, Abdullah J, Joachimiak A J Struct Funct Genomics. 2008 Dec;9(1-4):1-6. Epub 2008 Jun 20. PMID:18566914^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.