2z3x

Structure of a Protein-DNA Complex Essential for DNA Protection in Spore of Bacillus Species

spinqualitylabelsall models 2z3x, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2z3x is a 5 chain structure with sequence from Bacillus subtilis and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SSPC_BACSU SASP are bound to spore DNA. They are double-stranded DNA-binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The DNA-binding alpha/beta-type small acid-soluble proteins (SASPs) are a major factor in the resistance and long-term survival of spores of Bacillus species by protecting spore DNA against damage due to desiccation, heat, toxic chemicals, enzymes, and UV radiation. We now report the crystal structure at 2.1 A resolution of an alpha/beta-type SASP bound to a 10-bp DNA duplex. In the complex, the alpha/beta-type SASP adopt a helix-turn-helix motif, interact with DNA through minor groove contacts, bind to approximately 6 bp of DNA as a dimer, and the DNA is in an A-B type conformation. The structure of the complex provides important insights into the molecular details of both DNA and alpha/beta-type SASP protection in the complex and thus also in spores. Structure of a protein-DNA complex essential for DNA protection in spores of Bacillus species.,Lee KS, Bumbaca D, Kosman J, Setlow P, Jedrzejas MJ Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):2806-11. Epub 2008 Feb 19. PMID:18287075 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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