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Chlorobium limicola

ABSTRACT: Photosynthetic bacterium

PROVIDER: PRJNA35353 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	LMBR01.dat.gz	Other
	LMBR01.fasta.gz	Fasta.gz
	LMBR01.master.dat	Other

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Chlorobium phaeovibrioides

Project description:Nitrogen-fixing photosynthetic bacterium

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Chlorobium limicola DSM 245

Project description:A green sulfur bacterium used to model the reductive carbolic acid cycle.

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Chlorobium phaeobacteroides

Project description:Photosynthetic microorganism

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Crystallization, preliminary crystallographic analysis and phasing of the thiosulfate-binding protein SoxY from Chlorobium limicola f. thiosulfatophilum.

Project description:The 22 kDa SoxYZ protein complex from the green sulfur bacterium Chlorobium limicola f. thiosulfatophilum is a central player in the sulfur-oxidizing (Sox) enzyme system of the organism by activating thiosulfate for oxidation by SoxXA and SoxB. It has been proposed that SoxYZ exists as a heterodimer or heterotetramer, but the properties and role of the individual components of the complex thus far remain unknown. Here, the heterologous expression, purification, and the crystallization of stable tetrameric SoxY are reported. Crystals of SoxY diffract to 2.15 A resolution and belong to space group C222(1), with unit-cell parameters a = 41.22, b = 120.11, c = 95.30 A. MIRAS data from Pt(2+)- and Hg(2+)-derivatized SoxY crystals resulted in an interpretable electron-density map at 3 A resolution after density modification.

| S-EPMC2225222 | biostudies-literature

Structure of the light-harvesting bacteriochlorophyll c assembly in chlorosomes from Chlorobium limicola determined by solid-state NMR.

Project description:We have determined the atomic structure of the bacteriochlorophyll c (BChl c) assembly in a huge light-harvesting organelle, the chlorosome of green photosynthetic bacteria, by solid-state NMR. Previous electron microscopic and spectroscopic studies indicated that chlorosomes have a cylindrical architecture with a diameter of approximately 10 nm consisting of layered BChl molecules. Assembly structures in huge noncrystalline chlorosomes have been proposed based mainly on structure-dependent chemical shifts and a few distances acquired by solid-state NMR, but those studies did not provide a definite structure. Our approach is based on (13)C dipolar spin-diffusion solid-state NMR of uniformly (13)C-labeled chlorosomes under magic-angle spinning. Approximately 90 intermolecular C C distances were obtained by simultaneous assignment of distance correlations and structure optimization preceded by polarization-transfer matrix analysis. It was determined from the approximately 90 intermolecular distances that BChl c molecules form piggyback-dimer-based parallel layers. This finding rules out the well known monomer-based structures. A molecular model of the cylinder in the chlorosome was built by using this structure. It provided insights into the mechanisms of efficient light harvesting and excitation transfer to the reaction centers. This work constitutes an important advance in the structure determination of huge intact systems that cannot be crystallized.

| S-EPMC1783392 | biostudies-literature

Chlorobium limicola strain:Frasassi

Project description:Chlorobium limicola strain:Frasassi Genome sequencing and assembly

| PRJNA300282 | ENA

X-ray crystallographic analysis of the sulfur carrier protein SoxY from Chlorobium limicola f. thiosulfatophilum reveals a tetrameric structure.

Project description:Dissimilatory oxidation of thiosulfate in the green sulfur bacterium Chlorobium limicola f. thiosulfatophilum is carried out by the ubiquitous sulfur-oxidizing (Sox) multi-enzyme system. In this system, SoxY plays a key role, functioning as the sulfur substrate-binding protein that offers its sulfur substrate, which is covalently bound to a conserved C-terminal cysteine, to another oxidizing Sox enzyme. Here, we report the crystal structures of a stand-alone SoxY protein of C. limicola f. thiosulfatophilum, solved at 2.15 A and 2.40 A resolution using X-ray diffraction data collected at 100 K and room temperature, respectively. The structure reveals a monomeric Ig-like protein, with an N-terminal alpha-helix, that oligomerizes into a tetramer via conserved contact regions between the monomers. The tetramer can be described as a dimer of dimers that exhibits one large hydrophobic contact region in each dimer and two small hydrophilic interface patches in the tetramer. At the tetramer interface patch, two conserved redox-active C-terminal cysteines form an intersubunit disulfide bridge. Intriguingly, SoxY exhibits a dimer/tetramer equilibrium that is dependent on the redox state of the cysteines and on the type of sulfur substrate component bound to them. Taken together, the dimer/tetramer equilibrium, the specific interactions between the subunits in the tetramer, and the significant conservation level of the interfaces strongly indicate that these SoxY oligomers are biologically relevant.

| S-EPMC2203348 | biostudies-literature

Gloeobacter violaceus

Project description:Photosynthetic bacterium

| PRJNA35287 | ENA

Cyanobacterium stanieri

Project description:Photosynthetic bacterium

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Thiocystis violascens

Project description:Photosynthetic bacterium

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