Structure of the stand-alone RAM-domain protein fromThermus thermophilusHB8

Abstract

PDB Reference: TTHA0845, 2djw, r2djwsf.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 fold and it dimerizes mainly through interactions between the antiparallelsheets. 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 standalone RAM-domain proteins and the C-terminal RAM domains of Lrp/AsnCfamily proteins.

Interactions between the archaeal transcription repressor FL11 and its coregulators lysine and arginine

“…Among FFRPs so far crystallized, that is, LrpA,6 FL11,7, 8 AsnC,9 LrpC,9 TTHA0845,10 DM1,11 Lrp,12 NMB0573,13 MtbLrp (Rv3291c),14, 15 ST1022,16 and STS042,17 Lrp was crystallized without its coregulator leucine 12. Some others were crystallized with amino acids, but their roles in transcription regulation remain unclear.…”

Crystal structure of STS042, a stand‐alone RAM module protein, from hyperthermophilic archaeon Sulfolobus tokodaii strain7

“…These are classified as stand‐alone RAM‐domain (SARD) proteins 8, 9. The functions of these proteins remain unclear, though some of these are crystallized and structure determined 10–12. The structure of TTHA0845 from Thermus thermophilus , which is one of the SARD proteins, was determined in a unique homodecameric form 10.…”

“…The functions of these proteins remain unclear, though some of these are crystallized and structure determined 10–12. The structure of TTHA0845 from Thermus thermophilus , which is one of the SARD proteins, was determined in a unique homodecameric form 10. In one of the SARD proteins, DM1, self‐association to a hexadecamer and octamer is promoted by the addition of hydrophobic amino acids 13…”

Transcription Regulation by Feast/Famine Regulatory Proteins, FFRPs, in Archaea and Eubacteria

“…Although several FFRPs from archaea and eubacteria have been crystallized (Table 1), [7][8][9][10][11][12][13][14][15] FL11 remains as the single FFRP whose structure has been determined in complex with its target DNA. 7) A DNA duplex was included when crystallizing Lrp, but the DNA was disordered and not traced.…”

“…1). 9,14) FFRPs of this type are referred to as demi (DM-) FFRPs (Table 1). 12,16) Higher-order structures are formed by assembling dimers (Fig.…”