A possible disk to cylinder transition of assemblies of feast/famine regulatory proteins, FFRPs.

Koike, Hideaki; Sakuma, Michiyo; Mikami, Aya; Amano, Naoki; Suzuki, Masashi

doi:10.2183/pjab.79b.63

Cited by 24 publications

(37 citation statements)

References 18 publications

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“…FL11 (Leonard et al, 2001;Koike et al, 2004) and the SARD protein Pyrococcus sp. DM1 (Koike et al, 2003).…”

Section: Crystallization Data Processing and Structurementioning

confidence: 99%

“…DM1 (Leonard et al, 2001;Koike et al, 2003;Thaw et al, 2006) revealed that the four dimers are arranged as a disc. In the structure of the Pyrococcus sp.…”

Section: Crystallization Data Processing and Structurementioning

confidence: 99%

“…Archaea and bacteria also have proteins bearing the RAM domain, but lacking the DNA-binding domain. These are classified as stand-alone RAM-domain (SARD) proteins (Ettema et al, 2002), which are also called headless Lrp/AsnC proteins (Kudo et al, 2001) and demi-FFRPs (Koike et al, 2003), and their role has not yet been elucidated. It has been speculated that their function might be similar to that of E. coli IlvH, which is the ACT-containing small regulatory subunit of acetohydroxyacid synthase isozyme III (Mendel et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

“…DM1 and P. furiosus Q8U228, have been crystallized (Kudo et al, 2001;Agapay et al, 2005). The DM1 structure is similar to that of the C-terminal RAM domains of LrpA, LrpC and AsnC, with the four dimers arranged in a ring (Koike et al, 2003). In solution, DM1 adopts different oligomeric states depending on the presence or absence of effector molecules such as hydrophobic amino acids and some metabolic intermediates (Sakuma et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2006

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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.

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“…FL11 (Leonard et al, 2001;Koike et al, 2004) and the SARD protein Pyrococcus sp. DM1 (Koike et al, 2003).…”

Section: Crystallization Data Processing and Structurementioning

confidence: 99%

“…DM1 (Leonard et al, 2001;Koike et al, 2003;Thaw et al, 2006) revealed that the four dimers are arranged as a disc. In the structure of the Pyrococcus sp.…”

Section: Crystallization Data Processing and Structurementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

et al. 2006

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“…In fact, the tetrameric assembly form is most common among FFRPs in crystal as well as in solution: E. coli LRP, 15) LrpA, 16) and pot1216151 (DM1). 13), 14) In short, FL11 has multiple assembly forms, and the aim of this paper is to further characterize particles (i.e. possible tetrameric assemblies) formed in solution in the absence of DNA, partly by re-analyzing the cryo-electron micrographs.…”

Section: )mentioning

confidence: 99%

An electron microscopic study of the archaeal feast/famine regulatory protein

Ishijima

Clowney

Suzuki

2004

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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Abstract:Particles formed by a feast/famine regulatory protein (FFRP), pot0434017 (FL11), in solution in the absence of DNA were analyzed using electron microscopy (EM). By applying conventional (i.e. dry) EM to the protein negatively stained with uranyl acetate, top views of tetrameric assemblies of dimers were obtained, where four pairs each of N-domains were extending from C-domains assembled around the centers. In cryo-EM images of the protein embedded in 3D amorphous ice, sets of four densities were arranged around ellipsoids having similar lengths for their long axes but of different lengths for their short axes. These images were interpreted as projections with different tilts of four pairs of N-domains arranged inside flat assemblies: the positively charged N-domains only were stained with ammonium molybdate, but the negatively charged C-domains were unstained and thus unobservable. Using seventeen such cryo-images, in combination with a crystal structure equivalent to an assembly of C-domains, a disk-like 3D structure was reconstructed.

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