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CryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction
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DOI：10.1126/sciadv.1701264.png)
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Abstract
En 中文
Human dynamin-like, interferon-induced myxovirus resistance 2 (Mx2 or MxB) is a potent HIV-1 inhibitor. Antiviral activity requires both the amino-terminal region of MxB and protein oligomerization, each of which has eluded structural determination due to difficulties in protein preparation. We report that maltose binding protein-fused, full-length wild-type MxB purifies as oligomers and further self-assembles into helical arrays in physiological salt. Guanosine triphosphate (GTP), but not guanosine diphosphate, binding results in array disassembly, whereas subsequent GTP hydrolysis allows its reformation. Using cryo-electron microscopy (cryoEM), we determined the MxB assembly structure at 4.6 A resolution, representing the first near-atomic resolution structure in the mammalian dynamin superfamily. The structure revealed previously described and novel MxB assembly interfaces. Mutational analyses demonstrated a critical role for one of the novel interfaces in HIV-1 restriction.
Keywords:
MOLECULAR-DYNAMICS
HELICAL RECONSTRUCTION
VIRAL DETERMINANTS
PROTEIN
PREDICTION
GTPASE
MODEL
SPECIFICITY
RECOGNITION
HYDROLYSIS
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