1pcz | pdb_00001pcz

STRUCTURE OF TATA-BINDING PROTEIN

spinqualitylabelsall models 1pcz, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pcz is a 2 chain structure with sequence from "pyrococcus_furiosus_subsp._woesei"_kanoksilapatham_et_al._2004 "pyrococcus furiosus subsp. woesei" kanoksilapatham et al. 2004. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TBP_PYRWO] General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation. 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 This study analyzes the three-dimensional structure of the TATA-box binding protein (TBP) from the hyperthermophilic archaea Pyrococcus woesei. The crystal structure of P. woesei TBP (PwTBP) was solved at 2.2 A by X-ray diffraction and as expected from sequence homology (36% to 41% identical to eukaryotic TBPs) its overall structure is very similar to eukaryotic TBPs. The thermal unfolding transition temperature of this protein was measured by differential scanning calorimetry to be 101 degrees C, which is more than 40 degrees C higher than that of yeast TBP. Preliminary titration calorimetry data show that the affinity of PwTBP for its DNA target, unlike its eukaryotic counterparts, is enhanced by increasing the temperature and salt concentration. The structure reveals possible explanations for this thermostability and these unusual DNA binding properties. The crystal structure of this hyperthermostable protein was compared to its mesophilic homologs and analyzed for differences in the native structure that may contribute to thermostability. Differences found were: (1) a disulfide bond not found in mesophilic counterparts; (2) an increased number of surface electrostatic interactions; (3) more compact protein packing. The presumed DNA binding surface of PwTBP, like its eukaryotic counterparts, is hydrophobic but the electrostatic profile surrounding the protein is relatively neutral compared to the asymmetric positive potential that surrounds eukaryotic TBPs. The total reliance on a hydrophobic interface with DNA may explain the enhanced affinity of PwTBP for its DNA promoter at higher temperatures and increased salt concentration. The crystal structure of a hyperthermophilic archaeal TATA-box binding protein.,DeDecker BS, O'Brien R, Fleming PJ, Geiger JH, Jackson SP, Sigler PB J Mol Biol. 1996 Dec 20;264(5):1072-84. PMID:9000631 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TATA-binding protein 3D structures

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