1e0b | pdb_00001e0b

Chromo shadow domain from fission yeast swi6 protein.

spinqualitylabelsall models 1e0b, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1e0b is a 2 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: 1PG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SWI6_SCHPO Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes. 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 BACKGROUND: Proteins such as HP1, found in fruit flies and mammals, and Swi6, its fission yeast homologue, carry a chromodomain (CD) and a chromo shadow domain (CSD). These proteins are required to form functional transcriptionally silent centromeric chromatin, and their mutation leads to chromosome segregation defects. CSDs have only been found in tandem in proteins containing the related CD. Most HP1-interacting proteins have been found to associate through the CSD and many of these ligands contain a conserved pentapeptide motif. RESULTS: The 1.9 A crystal structure of the Swi6 CSD is presented here. This reveals a novel dimeric structure that is distinct from the previously reported monomeric nuclear magnetic resonance (NMR) structure of the CD from the mouse modifier 1 protein (MoMOD1, also known as HP1beta or M31). A prominent pit with a non-polar base is generated at the dimer interface, and is commensurate with binding an extended pentapeptide motif. Sequence alignments based on this structure highlight differences between CDs and CSDs that are superimposed on a common structural core. The analyses also revealed a previously unrecognised circumferential hydrophobic sash around the surface of the CD structure. CONCLUSIONS: Dimerisation through the CSD of HP1-like proteins results in the simultaneous formation of a putative protein-protein interaction pit, providing a potential means of targeting CSD-containing proteins to particular chromatin sites. Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis.,Cowieson NP, Partridge JF, Allshire RC, McLaughlin PJ Curr Biol. 2000 May 4;10(9):517-25. PMID:10801440 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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