2euv | pdb_00002euv

Principles of protein-DNA recognition revealed in the structural analysis of Ndt80-MSE DNA complexes

spinqualitylabelsall models 2euv, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2euv is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1mnn, 1mn4, 1m6u, 1m7u, 2etw, 2euw, 2eux, 2euz, 2evf, 2evg, 2evh, 2ehi, 2ehj Gene: ndt80 (Saccharomyces cerevisiae) Resources: FirstGlance, OCA, RCSB, PDBsum Function [NDT80_YEAST] Transcription factor required for successful completion of meiosis and spore formation. Gets activated after completion of meiotic recombination at the end of prophase I. Recognizes and binds to the middle sporulation element (MSE) 5'-C[AG]CAAA[AT]-3' in the promoter region of stage-specific genes that are required for progression through meiosis and sporulation. Competes for binding to MSE with the transcriptional repressor SUM1, which represses middle sporulation-specific genes during mitosis and early sporulation. 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 Saccharomyces cerevisiae transcription factor Ndt80 selectively binds a DNA consensus sequence (the middle sporulation element [MSE]) to activate gene expression after the successful completion of meiotic recombination. Here we report the X-ray crystal structures of Ndt80 bound to ten distinct MSE variants. Comparison of these structures with the structure of Ndt80 bound to a consensus MSE reveals structural principles that determine the DNA binding specificity of this transcription factor. The 5' GC-rich end of the MSE contains distinct 5'-YpG-3' steps that are recognized by arginine side chains through a combination of hydrogen bonding and cation-pi interactions. The 3' AT-rich region is recognized via minor groove contacts that sterically exclude the N2 atom of GC base pairs. The conformation of the AT-rich region is fixed by interactions with the protein that favor recognition of poly(A)-poly(T) versus mixed AT sequences through an avoidance of major groove steric clashes at 5'-ApT-3' steps. Principles of protein-DNA recognition revealed in the structural analysis of Ndt80-MSE DNA complexes.,Lamoureux JS, Glover JN Structure. 2006 Mar;14(3):555-65. PMID:16531239 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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