Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	De novo backbone trace of GroEL from single particle electron cryomicroscopy.
Journal, issue, pages	Structure, Vol. 16, Issue 3, Page 441-448, Year 2008
Publish date	Jun 10, 2008
Authors	Steven J Ludtke / Matthew L Baker / Dong-Hua Chen / Jiu-Li Song / David T Chuang / Wah Chiu /
PubMed Abstract	In this work, we employ single-particle electron cryo-microscopy (cryo-EM) to reconstruct GroEL to approximately 4 A resolution with both D7 and C7 symmetry. Using a newly developed skeletonization ...In this work, we employ single-particle electron cryo-microscopy (cryo-EM) to reconstruct GroEL to approximately 4 A resolution with both D7 and C7 symmetry. Using a newly developed skeletonization algorithm and secondary structure element identification in combination with sequence-based secondary structure prediction, we demonstrate that it is possible to achieve a de novo Calpha trace directly from a cryo-EM reconstruction. The topology of our backbone trace is completely accurate, though subtle alterations illustrate significant differences from existing crystal structures. In the map with C7 symmetry, the seven monomers in each ring are identical; however, the subunits have a subtly different structure in each ring, particularly in the equatorial domain. These differences include an asymmetric salt bridge, density in the nucleotide-binding pocket of only one ring, and small shifts in alpha helix positions. This asymmetric conformation is different from previous asymmetric structures, including GroES-bound GroEL, and may represent a "primed state" in the chaperonin pathway.
External links	Structure / PubMed:18334219
Methods	EM (single particle)
Resolution	4.2 - 4.7 Å
Structure data	5001 3cau EMDB-5001: Native, unliganded GroEL, D7 symmetrized, 4.2 A resolution 0.5 criterion PDB-3cau: D7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEM Method: EM (single particle) / Resolution: 4.2 Å 5002 3c9v EMDB-5002: Native, unliganded GroEL, C7 symmetrized, 4.7 A resolution 0.5 criterion PDB-3c9v: C7 Symmetrized Structure of Unliganded GroEL at 4.7 Angstrom Resolution from CryoEM Method: EM (single particle) / Resolution: 4.7 Å
Source	escherichia coli (E. coli)
Keywords	CHAPERONE / GroEL / ATP-binding / Cell cycle / Cell division / Nucleotide-binding / Phosphoprotein