2A5Z
Crystal Structure of Protein of Unknown Function SO2946 from Shewanella oneidensis MR-1
Summary for 2A5Z
Entry DOI | 10.2210/pdb2a5z/pdb |
Descriptor | hypothetical protein SO2946, MAGNESIUM ION (3 entities in total) |
Functional Keywords | shewanella oneidensis mr-1, hypothetical protein, so2946, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function |
Biological source | Shewanella oneidensis |
Total number of polymer chains | 3 |
Total formula weight | 83711.47 |
Authors | Nocek, B.,Bigelow, L.,Abdullah, J.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2005-07-01, release date: 2005-08-16, Last modification date: 2024-11-20) |
Primary citation | Nocek, B.,Bigelow, L.,Abdullah, J.,Joachimiak, A. Structure of SO2946 orphan from Shewanella oneidensis shows "jelly-roll" fold with carbohydrate-binding module. J.STRUCT.FUNCT.GENOM., 9:1-6, 2008 Cited by PubMed Abstract: 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. PubMed: 18566914DOI: 10.1007/s10969-008-9040-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.015 Å) |
Structure validation
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