2hax | pdb_00002hax

Crystal structure of Bacillus caldolyticus cold shock protein in complex with hexathymidine

spinqualitylabelsall models 2hax, resolution 1.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hax is a 4 chain structure with sequence from 'bacillus caldolyticus'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, MPD Related: 1c9o, 1csp, 1mjc, 2es2 Gene: cspB ('Bacillus caldolyticus') Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [CSPB_BACCL] Affects cell viability at low temperatures. 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 Bacterial cold shock proteins (CSPs) regulate cellular adaptation to cold stress. Functions ascribed to CSP include roles as RNA chaperones and in transcription antitermination. We present the crystal structure of the Bacillus caldolyticus CSP (Bc-Csp) in complex with hexathymidine (dT(6)) at a resolution of 1.29 A. Bound to dT(6), crystalline Bc-Csp forms a domain-swapped dimer in which beta strands 1-3 associate with strands 4 and 5 from the other subunit to form a closed beta barrel and vice versa. The globular units of dimeric Bc-Csp closely resemble the well-known structure of monomeric CSP. Structural reorganization from the monomer to the domain-swapped dimer involves a strictly localized change in the peptide bond linking Glu36 and Gly37 of Bc-Csp. Similar structural reorganizations have not been found in any other CSP or oligonucleotide/oligosaccharide-binding fold structures. Each dT(6) ligand is bound to one globular unit of Bc-Csp via an amphipathic protein surface. Individual binding subsites interact with the DNA bases through stacking and hydrogen bonding. The sugar-phosphate backbone remains solvent exposed. Based on crystallographic and biochemical studies of deoxyoligonucleotide binding to CSP, we suggest a common mode of binding of single-stranded heptanucleotide motifs to proteins containing cold shock domains, including the eukaryotic Y-box factors. Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus.,Max KE, Zeeb M, Bienert R, Balbach J, Heinemann U FEBS J. 2007 Mar;274(5):1265-79. Epub 2007 Jan 31. PMID:17266726 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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