2elk

Solution structure of the SANT domain of fission yeast SPCC24B10.08c protein

spinqualitylabelsall models 2elk Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2elk is a 1 chain structure with sequence from Schizosaccharomyces pombe. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function ADA2_SCHPO Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B (By similarity). Required for full activation of chromatin alteration and meiotic recombination at meiotic recombination hot spot ade6-M26. Also required for the regulation of transcription and chromatin structure around ade6-M26 in response to osmotic stress. Needed for hyperacetylation of histone H3 around ade6-M26. [UniProtKB:Q02336] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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