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	Native structure of a retroviral envelope protein and its conformational change upon interaction with the target cell.
Journal, issue, pages	J Struct Biol, Vol. 197, Issue 2, Page 172-180, Year 2017
Publish date	Jun 23, 2016
Authors	Christiane Riedel / Daven Vasishtan / C Alistair Siebert / Cathy Whittle / Maik J Lehmann / Walther Mothes / Kay Grünewald /
PubMed Abstract	Enveloped viruses enter their host cells by membrane fusion. The process of attachment and fusion in retroviruses is mediated by a single viral envelope glycoprotein (Env). Conformational changes of ...Enveloped viruses enter their host cells by membrane fusion. The process of attachment and fusion in retroviruses is mediated by a single viral envelope glycoprotein (Env). Conformational changes of Env in the course of fusion are a focus of intense studies. Here we provide further insight into the changes occurring in retroviral Env during its initial interaction with the cell, employing murine leukemia virus (MLV) as model system. We first determined the structure of both natively membrane anchored MLV Env and MLV Env tagged with YFP in the proline rich region (PRR) by electron cryo tomography (cET) and sub-volume averaging. At a resolution of ∼20Å, native MLV Env presents as a hollow trimer (height ∼85Å, diameter ∼120Å) composed of step-shaped protomers. The major difference to the YFP-tagged protein was in regions outside of the central trimer. Next, we focused on elucidating the changes in MLV Env upon interaction with a host cell. Virus interaction with the plasma membrane occurred over a large surface and Env clustering on the binding site was observed. Sub-volume averaging did yield a low-resolution structure of Env interacting with the cell, which had lost its threefold symmetry and was elongated by ∼35Å in comparison to the unbound protein. This indicates a major rearrangement of Env upon host cell binding. At the site of virus interaction, the otherwise clearly defined bilayer structure of the host cell plasma membrane was much less evident, indicative of integral membrane protein accumulation and/or a change in membrane lipid composition.
External links	J Struct Biol / PubMed:27345930 / PubMed Central
Methods	EM (subtomogram averaging)
Resolution	15.0 - 22.0 Å
Structure data	EMDB-3357: electron density map of murine leukaemia virus envelope glycoprotein tagged in the proline rich region with YFP as reconstructed by subtomogram averaging on viruses produced in DFJ8 cells Method: EM (subtomogram averaging) / Resolution: 20.0 Å EMDB-3363: electron density map of murine leukaemia virus envelope glycoprotein tagged in the proline rich region with YFP as reconstructed by subtomogram averaging on murine leukemia virus virus like particles (3 plasmid system) produced in COS1 cells Method: EM (subtomogram averaging) / Resolution: 22.0 Å EMDB-3365: electron density map of murine leukaemia virus envelope glycoprotein as reconstructed by subtomogram averaging on murine leukemia virus virus like particles (3 plasmid system) produced in COS1 cells Method: EM (subtomogram averaging) / Resolution: 22.0 Å EMDB-3373: electron density map of murine leukaemia virus envelope glycoprotein as reconstructed by subtomogram averaging applying a mask on 1 protomer on murine leukemia virus particles and virus like particles and applying 3fold symmetry to the single protomer afterwards Method: EM (subtomogram averaging) / Resolution: 15.0 Å
Source	Murine leukemia virus