1vto

1.9 A RESOLUTION REFINED STRUCTURE OF TBP RECOGNIZING THE MINOR GROOVE OF TATAAAAG

spinqualitylabelsall models 1vto, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1vto is a 6 chain structure with sequence from Arabidopsis thaliana 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 1.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TBP1_ARATH General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Publication Abstract from PubMed The three-dimensional structure of a TATA box-binding protein (TBP) from Arabidopsis thaliana complexed with a fourteen base pair oligonucleotide bearing the Adenovirus major late promoter TATA element has been refined at 1.9 A resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped alpha/beta protein induces an unprecedented conformational change in the DNA. A detailed structural and functional analysis of this unusual protein-DNA complex is presented, with particular emphasis on the mechanisms of DNA deformation, TATA element recognition, and preinitiation complex assembly. 1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAAG.,Kim JL, Burley SK Nat Struct Biol. 1994 Sep;1(9):638-53. PMID:7634103 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TATA-binding protein 3D structures

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