1nmf | pdb_00001nmf

MAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES

spinqualitylabelsall models 1nmf, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nmf is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1nmg Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CSPB_BACSU] Binds to the pentamer sequences ATTGG and CCAAT with highest affinity in single-stranded DNA, and also to other sequences. Has greater affinity for ATTGG than CCAAT. Can act as transcriptional activator of cold shock genes by recognizing putative ATTGG-box elements present in promoter regions of genes induced under cold shock conditions. 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 cold-shock domain (CSD) is found in many eukaryotic transcriptional factors and is responsible for the specific binding to DNA of a cis-element called the Y-box. The same domain exists in the sequence of the Xenopus RNA-binding proteins FRG Y1 and FRG Y2 (refs 1, 3). The major cold-shock proteins of Escherichia coli (CS7.4) and B. subtilis (CspB) have sequences that are more than 40 per cent identical to the cold-shock domain. We present here the three-dimensional structure of CspB determined by nuclear magnetic resonance spectroscopy. The 67-residue protein consists of an antiparallel five-stranded beta-barrel with strands connected by turns and loops. The structure resembles that of staphylococcal nuclease and the gene-5 single-stranded-DNA-binding protein. A three-stranded beta-sheet, which contains the conserved RNA-binding motif RNP1 as well as a motif similar to RNP2 in two neighbouring antiparallel beta-strands, has basic and aromatic residues at its surface which could serve as a binding site for single-stranded DNA. CspB binds to single-stranded DNA in gel retardation experiments. Structure in solution of the major cold-shock protein from Bacillus subtilis.,Schnuchel A, Wiltscheck R, Czisch M, Herrler M, Willimsky G, Graumann P, Marahiel MA, Holak TA Nature. 1993 Jul 8;364(6433):169-71. PMID:8321289 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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