Journal of Structural and Functional Genomics

, Volume 9, Issue 1, pp 1–6

Structure of SO2946 orphan from Shewanella oneidensis shows “jelly-roll” fold with carbohydrate-binding module


DOI: 10.1007/s10969-008-9040-0

Cite this article as:
Nocek, B., Bigelow, L., Abdullah, J. et al. J Struct Funct Genomics (2008) 9: 1. doi:10.1007/s10969-008-9040-0


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 Å 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.


Jelly-roll topologyCarbohydrate-binding modulesOrphan proteinMagnesium bindingSAD phasingSingleton

Copyright information

© Springer Science+Business Media B.V 2008

Authors and Affiliations

  • B. Nocek
    • 1
  • L. Bigelow
    • 1
  • J. Abdullah
    • 1
  • A. Joachimiak
    • 1
    • 2
  1. 1.Midwest Center for Structural Genomics and Structural Biology Center, Biosciences DivisionArgonne National LaboratoryArgonneUSA
  2. 2.Department of Biochemistry and Molecular BiologyUniversity of ChicagoChicagoUSA