Database: PDB / ID: 2i68|
|Title||Cryo-EM based theoretical model structure of transmembrane domain of the multidrug-resistance antiporter from E. coli EmrE|
|Keywords||TRANSPORT PROTEIN / transmembrane protein / small-multidrug resistance / transporter / homodimer / dual topology|
|Specimen source||Escherichia coli / bacteria /|
|Method||Electron crystallography (Crystallography / Vitreous ice (cryo EM))|
|Authors||Fleishman, S.J. / Harrington, S.E. / Enosh, A. / Halperin, D. / Tate, C.G. / Ben-Tal, N.|
|Citation||J. Mol. Biol., 2006, 364, 54-67|
primary. J. Mol. Biol., 2006, 364, 54-67 StrPapers
#1. Embo J., 2003, 22, 6175-6181 StrPapers
|Date||Deposition: Aug 28, 2006 / Release: Oct 3, 2006 / Last modification: Feb 24, 2009|
|3D viewer|| / |
Downloads & links
A: Protein emrE
B: Protein emrE
30.4 kDa, 2 molecules
|#1||idetical with deposited unit / defined by author / Symmetry operations: (identity)x1|
|Experiment||Method: ELECTRON CRYSTALLOGRAPHY|
|EM experiment||Reconstruction method: CRYSTALLOGRAPHY / Specimen type: VITREOUS ICE (CRYO EM)|
|Assembly of specimen||Aggregation state: 2D CRYSTAL|
|Radiation||Diffraction protocol: SINGLE WAVELENGTH / Monochromatic or laue m l: M / Scattering type: x-ray|
|Radiation wavelength||Relative weight: 1|
|3D reconstruction||Details: Canonical alpha-helices were fitted into a cryo-EM structure of EmrE at 6Angstroms in-plane and 16Angstroms vertical resolution. The sequence segments were assigned based on biophysical and sequence data as elaborated in the principal citation. The orientation of each helix around its principal axis was set using evolutionary conservation, requiring that evolutionarily conserved positions be packed inside the core of the protein, whereas variable residues face the outside. A kink was introduced in helix C to fit a bend in the cryo-EM structure and according to sequence clues (see principal citation). A full description of potential inaccuracies in the model is presented in the principal citation. In brief, these include the following: the vertical positioning of the helices may be wrong by several Angstroms due to the low vertical resolution of the cryo-EM structure; the orientations of the helices around their principal axes may vary by about 20 degrees; the positions of backbone atoms on the terminal turns of each helix may not conform to alpha-helical ideality as assumed in the model structure.|
|Number of atoms included #LAST||Protein: 624 / Nucleic acid: 0 / Ligand: 0 / Solvent: 0 / Total: 624|
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