5UOT

CryoEM structure of the helical assembly of full length MxB

This is a non-PDB format compatible entry.

Summary for 5UOT

• Entry DOI: 10.2210/pdb5uot/pdb
• EMDB information: 8577
• Descriptor: Interferon-induced GTP-binding protein Mx2 (1 entity in total)
• Functional Keywords: cryoem, mx2, mxb, assembly, interferon, hiv-1, dynamin, helical reconstruction, molecular dynamic simulation, antiviral protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 62
• Total formula weight: 4400745.00

Authors

Perilla, J.R.,Alvarez, F.J.D.,Zhang, P.,Schulten, K. (deposition date: 2017-02-01, release date: 2018-02-21, Last modification date: 2024-05-15)

Primary citation

Alvarez, F.J.D.,He, S.,Perilla, J.R.,Jang, S.,Schulten, K.,Engelman, A.N.,Scheres, S.H.W.,Zhang, P.
CryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction.
Sci Adv, 3:e1701264-e1701264, 2017

PubMed Abstract: 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.

PubMed: 28929138
DOI: 10.1126/sciadv.1701264

Experimental method

ELECTRON MICROSCOPY (4.6 Å)