Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8.
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.
Nakano
Noboru
N
RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Okazaki
Nobuo
N
Satoh
Shinya
S
Takio
Koji
K
Kuramitsu
Seiki
S
Shinkai
Akeo
A
Yokoyama
Shigeyuki
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D019281:Dimerization; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary / Q000235:genetics; D016963:Thermus thermophilus / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins