4JGS
Crystal structure of the xmrv tm retroviral fusion core
Summary for 4JGS
| Entry DOI | 10.2210/pdb4jgs/pdb |
| Related | 4JF3 4JPR |
| Descriptor | MLV-related proviral Env polyprotein, CHLORIDE ION (3 entities in total) |
| Functional Keywords | six helix bundle, viral-host membrane fusion, xmrv tm, viral surface, viral protein |
| Biological source | Mus musculus (mouse) |
| Cellular location | Transmembrane protein: Virion membrane; Single-pass type I membrane protein. Surface protein: Virion membrane; Peripheral membrane protein: P10404 |
| Total number of polymer chains | 9 |
| Total formula weight | 102796.17 |
| Authors | Cook, J.D.,Aydin, H.,Lee, J.E. (deposition date: 2013-03-02, release date: 2013-10-23, Last modification date: 2024-11-20) |
| Primary citation | Aydin, H.,Cook, J.D.,Lee, J.E. Crystal structures of Beta- and gammaretrovirus fusion proteins reveal a role for electrostatic stapling in viral entry. J.Virol., 88:143-153, 2014 Cited by PubMed Abstract: Membrane fusion is a key step in the life cycle of all envelope viruses, but this process is energetically unfavorable; the transmembrane fusion subunit (TM) of the virion-attached glycoprotein actively catalyzes the membrane merger process. Retroviral glycoproteins are the prototypical system to study pH-independent viral entry. In this study, we determined crystal structures of extramembrane regions of the TMs from Mason-Pfizer monkey virus (MPMV) and xenotropic murine leukemia virus-related virus (XMRV) at 1.7-Å and 2.2-Å resolution, respectively. The structures are comprised of a trimer of hairpins that is characteristic of class I viral fusion proteins and now completes a structural library of retroviral fusion proteins. Our results allowed us to identify a series of intra- and interchain electrostatic interactions in the heptad repeat and chain reversal regions. Mutagenesis reveals that charge-neutralizing salt bridge mutations significantly destabilize the postfusion six-helix bundle and abrogate retroviral infection, demonstrating that electrostatic stapling of the fusion subunit is essential for viral entry. Our data indicate that salt bridges are a major stabilizing force on the MPMV and XMRV retroviral TMs and likely provide the key energetics for viral and host membrane fusion. PubMed: 24131724DOI: 10.1128/JVI.02023-13 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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