0th PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author Manuscript NIH Figure 2 The comparison with the SF2 helicase Vasa shows that the ATPase CHD1 slot is open and not organized properly for the crystal structure of the ATP hydrolysis of PXD101 Belinostat the RNA helicase Vasa, the PDB code 2DB3. The ATP analogue AMP PNP-ATPase in the slot is represented as gray spheres. Helicase motif VI of the second lobe ATPase is green, with two arginine residues in question are fingers, R579 and R582, shown as a magenta stick and Sph Ren. The ATPase CHD1 motor. The color is Similar, with the ATP analogue ATP S γ shown as gray, the region corresponding to motif VI green helicase and C positions of two arginine residues in accordance with the arginine finger Vasa additional magenta Sph Ren.
One specific SWI2/SNF2 COLUMNS On the second cloth ATPase are gray. A schematic diagram showing the ATPase CHD1 split open by Vasa. CHD1 motor transformation to match the tight organization of the Vasa was a closing UNG the slot 52 ° ATPase. In contrast GSK2126458 to the structure of the hydrolysis, states closed Requests reference requests getting observed for Vasa, it has opened to CHD1 does not allow two arginine motif VI through directly to the phosphate tail of the bound nucleotide. See also Figure S2. Hauk et al. Mol Cell page 16 Author manuscript, increases available in PMC 10th September 2011.
PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author Manuscript NIH Figure 3 A propeller acid S To contact the motor ATPase double chromodomains representations of a predicted DNA-binding site of the surface Surface of the electrostatic double layer chromodomains, ATPase motor and better relations between the link helicopters Chromodomains valley of the flap and ATPase secondly, with the carbon atoms of the S Urereste that red red spheres. The electrostatic surface Chemical potentials have been demonstrated using APBS and shown in the range 5.0 kBT / e with the positive and negative potential as red and blue surface Chen. The sequence alignment of the helix S of the loading area Acid, which is in contact chromosome is the second cam ATPase in the crystal structure. Hauk et al. Mol Cell page 17 Author manuscript, increases available in PMC 10th September 2011. PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author Manuscript NIH A look at the surface Surface of the predicted DNA-binding ATPase in the second ply.
The structural core of three SF2 ATPases with their nucleic acid substrates, HEL308 connected: DNA, PDB code 2P6R green NS3: DNA, PDB code 2F55 were blue cloth on the second ATPase CHD1 superimposed. Only nucleic Depicted acid substrates. The surface chemical Of the second lobe ATPase, which is less than 5 Å Chromodom Ne S Acid of the helix as the Orange footprint. Hauk et al. Mol Cell page 18 Author manuscript, increases available in PMC 10th September 2011. PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author Manuscript NIH Figure 4 The wild-type interface Chromodom Ne ATPase is targeted for discrimination schematic structure of the substrate required S. cerevisiae crystal, highlighting the Residues Walls for mutagenesis. Schematic representations of S.
cerevisiae constructs used for biochemical analysis. ATPase in the presence of buffer alone, as measured naked DNA or mononucleosome substrates, is coupled using an assay NADH. A 206 bp DNA fragment containing the 601 base sequence positioning of nucleosomes at one end of a DNA was alone and mononucleosome substrates. All experiments were performed three times or Fter performed and presented as means with standard errors. Hauk et al. Mol Cell page 19 Author manuscript, increases available in PMC 10th September 2011. PA Author Manuscript NIH-PA Author Manuscript NIH Author Manuscript NIH-PA See also Figure S3. Hauk et al. Mol Cell page 20 Author manuscript, increases available in PMC 10th September 2011. PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author Manuscript NIH Figure 5 The St Tion of the interface Chromodom Ne ATPase improves the binding of DNA to the