5lmy

From Proteopedia

Solution structure of the m-pmv myristoylated matrix protein

PDB ID 5lmy

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Structural highlights

5lmy is a 1 chain structure with sequence from Mason-Pfizer monkey virus. This structure supersedes the now removed PDB entry 2lpy. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAG_MPMV p10 is the matrix protein. P14 is the nucleocapsid protein. p27 is the capsid protein.

Publication Abstract from PubMed

Matrix proteins play a key role in the transport of retroviral proteins inside infected cells and in the interaction with cellular membranes. In most retroviruses, retroviral matrix proteins are N-terminally myristoylated. This modification serves as a membrane targeting signal and also as an anchor for the membrane interaction. The aim of this work was to characterize interactions anchoring retroviral matrix protein at the plasma membrane of infected cell. To address this issue, we compared the structures and membrane affinity of the Mason-Pfizer monkey virus (M-PMV) wild-type matrix protein with its two budding deficient double mutants, i.e. T41I/T78I and Y28F/Y67F. The structures of the mutants were determined using solution NMR spectroscopy and their interactions with water-soluble phospholipids were studied. Water-soluble phospholipids are widely used models for studying membrane interactions by solution NMR spectroscopy. However, this approach might lead to artificial results due to unnatural hydrophobic interactions. Therefore, we used a new approach based on the measurement of the loss of the 1H NMR signal intensity of the protein sample induced by the addition of the liposomes containing phospholipids with naturally long fatty acids. HIV-1 matrix protein was used as a positive control because its ability to interact with liposomes has already been described. We found that in contrast to HIV-1, the M-PMV matrix protein interacted with the liposomes differently and much weaker. In our in-vivo experiments, the M-PMV matrix protein did not co-localize with lipid rafts. Therefore, we concluded that M-PMV might adopt different membrane binding mechanism than HIV-1.

Membrane interactions of the Mason-Pfizer monkey virus matrix protein and its budding deficient mutants.,Kroupa T, Langerova H, Dolezal M, Prchal J, Spiwok V, Hunter E, Rumlova M, Hrabal R, Ruml T J Mol Biol. 2016 Oct 7. pii: S0022-2836(16)30425-9. doi:, 10.1016/j.jmb.2016.10.010. PMID:27725181^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kroupa T, Langerova H, Dolezal M, Prchal J, Spiwok V, Hunter E, Rumlova M, Hrabal R, Ruml T. Membrane interactions of the Mason-Pfizer monkey virus matrix protein and its budding deficient mutants. J Mol Biol. 2016 Oct 7. pii: S0022-2836(16)30425-9. doi:, 10.1016/j.jmb.2016.10.010. PMID:27725181 doi:http://dx.doi.org/10.1016/j.jmb.2016.10.010