The presence of protein and DNA in the crystals was demonstrated by Raman spectroscopy. These crystals diffract to maximal resolutions of 1.78 and 1.29 Å, respectively. Crystals with Bc-Csp grew in the primitive orthorhombic space group P2 12 12, with unit-cell parameters a = 74.3, b = 64.9, c = 31.2 Å. Crystals of (dT) 6 with Bs-CspB grew in the orthorhombic space group C222 1, with unit-cell parameters a = 49.0, b = 53.2, c = 77.0 Å.
Bs-CspB ( M r = 7365) and Bc-Csp ( M r = 7333) were crystallized in the presence of the deoxyhexanucleotide (dT) 6. The major cold-shock proteins of Bacillus subtilis ( Bs-CspB) and Bacillus caldolyticus ( Bc-Csp) are small oligonucleotide/oligosaccharide-binding (OB) fold proteins that have been described as binding single-stranded nucleic acids. It is characterized by distinct changes in intracellular protein patterns whereby a set of cold-shock-inducible proteins become abundant. This study reveals the stoichiometry and sequence determinants of the binding of single-stranded nucleic acids to a preformed site on Bs-CspB and thus provides the structural basis of the RNA chaperone and transcription antitermination activities of the CSP.The cold-shock response has been described for several bacterial species. Fluorescence titration experiments monitoring the binding of oligopyrimidines to Bs-CspB reveal binding preferences at individual subsites and allow the design of an optimised heptapyrimidine ligand, which is bound with sub-nanomolar affinity. The sugar-phosphate backbone and the methyl groups of the thymine nucleobases remain solvent exposed and are not contacted by protein groups. 905 Likes, 22 Comments - RUDIMENTAL (rudimentaluk) on Instagram: Our new single is here, 'Jumper' feat. Explore our wide range of insurance policies for. Individual binding subsites interact with single nucleobases through stacking interactions and hydrogen bonding. General Insurance Online: ICICI Lombard is among Indias leading general insurance companies in India. Bs-CspB binds to dT 6 with nanomolar affinity via an amphipathic interface on the protein surface.
Here we present the structure of the Bacillus subtilis CspB ( Bs-CspB) in complex with hexathymidine (dT 6) at a resolution of 1.78 Å. They bind to single-stranded nucleic acids with a K D value in the micro- to nanomolar range. Bacterial cold shock proteins (CSPs) are involved in cellular adaptation to cold stress.
0 kommentar(er)
