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  • Title: Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8.
    Author: Nakano N, Okazaki N, Satoh S, Takio K, Kuramitsu S, Shinkai A, Yokoyama S.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2006 Sep 01; 62(Pt 9):855-60. PubMed ID: 16946463.
    Abstract:
    The stand-alone RAM (regulation of amino-acid metabolism) domain protein SraA from Thermus thermophilus HB8 (TTHA0845) was crystallized in the presence of zinc ions. The X-ray crystal structure was determined using a multiple-wavelength anomalous dispersion technique and was refined at 2.4 A resolution to a final R factor of 25.0%. The monomeric structure is a betaalphabetabetaalphabeta fold and it dimerizes mainly through interactions between the antiparallel beta-sheets. Furthermore, five SraA dimers form a ring with external and internal diameters of 70 and 20 A, respectively. This decameric structure is unique compared with the octameric and dodecameric structures found for other stand-alone RAM-domain proteins and the C-terminal RAM domains of Lrp/AsnC-family proteins.
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