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TitleCryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction.
Journal, issue, pagesSci Adv, Vol. 3, Issue 9, Page e1701264, Year 2017
Publish dateSep 15, 2017
AuthorsFrances J D Alvarez / Shaoda He / Juan R Perilla / Sooin Jang / Klaus Schulten / Alan N Engelman / Sjors H W Scheres / Peijun Zhang /
PubMed AbstractHuman 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, ...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 Å 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.
External linksSci Adv / PubMed:28929138 / PubMed Central
MethodsEM (helical sym.)
Resolution4.6 Å
Structure data

8577

5uot

EMDB-8577, PDB-5uot:
CryoEM structure of the helical assembly of full length MxB
Method: EM (helical sym.) / Resolution: 4.6 Å

Source
  • homo sapiens (human)
KeywordsANTIVIRAL PROTEIN / cryoEM / mx2 / mxb / assembly / interferon / hiv-1 / dynamin / helical reconstruction / Molecular dynamic simulation

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