3tek

ThermoDBP: a non-canonical single-stranded DNA binding protein with a novel structure and mechanism

spinqualitylabelsall models 3tek, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tek is a 2 chain structure with sequence from Thermoproteus tenax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: Ttx1576 (Thermoproteus tenax) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed ssDNA-binding proteins (SSBs) based on the oligonucleotide-binding fold are considered ubiquitous in nature and play a central role in many DNA transactions including replication, recombination, and repair. We demonstrate that the Thermoproteales, a clade of hyperthermophilic Crenarchaea, lack a canonical SSB. Instead, they encode a distinct ssDNA-binding protein that we term "ThermoDBP," exemplified by the protein Ttx1576 from Thermoproteus tenax. ThermoDBP binds specifically to ssDNA with low sequence specificity. The crystal structure of Ttx1576 reveals a unique fold and a mechanism for ssDNA binding, consisting of an extended cleft lined with hydrophobic phenylalanine residues and flanked by basic amino acids. Two ssDNA-binding domains are linked by a coiled-coil leucine zipper. ThermoDBP appears to have displaced the canonical SSB during the diversification of the Thermoproteales, a highly unusual example of the loss of a "ubiquitous" protein during evolution. Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales.,Paytubi S, McMahon SA, Graham S, Liu H, Botting CH, Makarova KS, Koonin EV, Naismith JH, White MF Proc Natl Acad Sci U S A. 2011 Nov 21. PMID:22106294 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Single-stranded DNA-binding protein

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