|Entry||Database: EMDB / ID: 1135|
|Title||Quaternary polymorphism of replicative helicase G40P: structural mapping and domain rearrangement.|
|Map data||Bacteriophage SPP1 helicase G40P: C6 architecture|
|Sample||C6 architecture of Bacteriophage SPP1 replicative helicase G40P:|
|Source||Bacillus phage SPP1 (bacteriophage)|
|Method||single particle reconstruction / negative staining / 24 Å resolution|
|Authors||Nunez-Ramirez R / Robledo Y / mesa P / Alonso JC / Carazo JM / Donate LE|
|Citation||Journal: J. Mol. Biol. / Year: 2006|
Title: Quaternary polymorphism of replicative helicase G40P: structural mapping and domain rearrangement.
Authors: Rafael Núñez-Ramírez / Yolanda Robledo / Pablo Mesa / Silvia Ayora / Juan Carlos Alonso / José María Carazo / Luis Enrique Donate
Abstract: Quaternary polymorphism is a distinctive structural feature of the DnaB family of replicative DNA hexameric helicases. The Bacillus subtilis bacteriophage SPP1 gene 40 product (G40P) belongs to this ...Quaternary polymorphism is a distinctive structural feature of the DnaB family of replicative DNA hexameric helicases. The Bacillus subtilis bacteriophage SPP1 gene 40 product (G40P) belongs to this family. Three different quaternary states have been described for G40P homohexamers, two of them with C(3) symmetry, and the other with C(6) symmetry. We present three-dimensional reconstructions of the different architectures of G40P hexamers and a variant lacking the N-terminal domain. Comparison of the G40P and the deletion mutant structures sheds new light on the functional roles of the N and C-terminal domains, at the same time that it allows the direct structural mapping of these domains. Based on this new information, hybrid EM/X-ray models are presented for all the different symmetries. These results suggest that quaternary polymorphism of hexameric helicases may be implicated in the translocation along the DNA.
|Date||Deposition: Jul 13, 2005 / Header (metadata) release: Jul 14, 2005 / Map release: May 16, 2006 / Last update: Oct 24, 2012|
|Structure viewer||EM map: |
Downloads & links
|File||emd_1135.map.gz (map file in CCP4 format, 2001 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 4.1 Å|
CCP4 map header:
-Entire C6 architecture of Bacteriophage SPP1 replicative helicase G40P
|Entire||Name: C6 architecture of Bacteriophage SPP1 replicative helicase G40P|
Oligomeric State: Homohexamer / Number of components: 1
|Mass||Theoretical: 300 kDa / Experimental: 300 kDa / Measured by: gel filtration chromatography|
-Component #1: protein, helicase
|Protein||Name: helicase / Oligomeric Details: Hexamer / Recombinant expression: Yes / Number of Copies: 6|
|Mass||Theoretical: 300 kDa / Experimental: 300 kDa|
|Source||Species: Bacillus phage SPP1 (bacteriophage) / Strain: SPP1|
|Source (engineered)||Expression System: Escherichia coli (E. coli) / Vector: pCB506|
|Source (natural)||Cell: Bacteria|
|Specimen||Specimen state: particle / Method: negative staining|
|Sample solution||Specimen conc.: 0.2 mg/ml|
Buffer solution: 50mM HEPES, 50mM NaCl, 10mM MgCl2, 1mM ATP, 1mM dithithreitol
|Support film||collodion/carbon coated 400 mesh copper grid|
|Staining||Grids with adsorbed protein satined on 2% uranyl acetate for 1 minute|
|Vitrification||Cryogen name: NONE|
-Electron microscopy imaging
|Imaging||Microscope: JEOL 2000EX|
|Electron gun||Electron source: TUNGSTEN HAIRPIN / Accelerating voltage: 80 kV / Electron dose: 20 e/Å2 / Illumination mode: OTHER|
|Lens||Magnification: 60000 X (nominal) / Imaging mode: OTHER|
|Specimen Holder||Holder: Eucentric / Model: OTHER|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Number of digital images: 40 / Scanner: ZEISS SCAI / Sampling size: 21 microns / Bit depth: 8|
|Processing||Method: single particle reconstruction / Number of projections: 700 / Applied symmetry: C6 (6 fold cyclic)|
|3D reconstruction||Algorithm: Random Conical / Software: SPIDER Xmipp / Resolution: 24 Å / Resolution method: FSC 0.5|
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