Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8

Journal Article · Fri Sep 01 04:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106031150· OSTI ID:22360163

Nakano, Noboru; Okazaki, Nobuo; Satoh, Shinya; Takio, Koji ^[1]; Kuramitsu, Seiki ^[1]; Shinkai, Akeo ^[1]; Yokoyama, Shigeyuki ^[1]

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1. RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148 (Japan)

The crystal structure of the stand-alone RAM domain from T. thermophilus HB8 has been determined at 2.4 Å resolution. The structure revealed that five dimers are arranged to form a ring. 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 Å resolution to a final R factor of 25.0%. The monomeric structure is a βαββαβ fold and it dimerizes mainly through interactions between the antiparallel β-sheets. Furthermore, five SraA dimers form a ring with external and internal diameters of 70 and 20 Å, 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.

• OSTI ID: 22360163
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 9 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTAL STRUCTURE
DIMERS
DISPERSIONS
INTERACTIONS
PROTEINS
R FACTORS
RESOLUTION
RINGS
WAVELENGTHS