6g0l | pdb_00006g0l

Structure of two molecules of the chromatin remodelling enzyme Chd1 bound to a nucleosome

Loading... Status: waiting for Mol* initialization Structural highlights 6g0l is a 12 chain structure with sequence from Saccharomyces cerevisiae S288C, Xenopus laevis and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 10Å Ligands: ADP, BEF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q92133_XENLA Publication Abstract from PubMed ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein-DNA interactions. Here we present structures of the Saccharomyces cerevisiae Chd1 protein engaged with nucleosomes in the presence of the transition state mimic ADP-beryllium fluoride. The path of DNA strands through the ATPase domains indicates the presence of contacts conserved with single strand translocases and additional contacts with both strands that are unique to Snf2 related proteins. The structure provides connectivity between rearrangement of ATPase lobes to a closed, nucleotide bound state and the sensing of linker DNA. Two turns of linker DNA are prised off the surface of the histone octamer as a result of Chd1 binding, and both the histone H3 tail and ubiquitin conjugated to lysine 120 are re-orientated towards the unravelled DNA. This indicates how changes to nucleosome structure can alter the way in which histone epitopes are presented. Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome.,Sundaramoorthy R, Hughes AL, El-Mkami H, Norman DG, Ferreira H, Owen-Hughes T Elife. 2018 Aug 6;7. pii: 35720. doi: 10.7554/eLife.35720. PMID:30079888 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chromodomain-helicase-DNA-binding protein 3D structures Helicase 3D structures

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