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4JF3

Crystal structure of the mpmv tm retroviral fusion core

Summary for 4JF3
Entry DOI10.2210/pdb4jf3/pdb
Related4JGS 4JPR
DescriptorEnvelope glycoprotein, CHLORIDE ION (3 entities in total)
Functional Keywordssix-helix bundle, fusion, mpmv tm, virus envelope, viral protein
Biological sourceMason-Pfizer monkey virus (MPMV)
Cellular locationTransmembrane protein: Virion membrane; Single-pass type I membrane protein (By similarity). Surface protein: Virion membrane; Peripheral membrane protein: P07575
Total number of polymer chains2
Total formula weight22935.98
Authors
Cook, J.D.,Aydin, H.,Lee, J.E. (deposition date: 2013-02-27, release date: 2013-10-23, Last modification date: 2024-11-20)
Primary citationAydin, 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: 24131724
DOI: 10.1128/JVI.02023-13
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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건을2025-07-23부터공개중

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