{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Alvarez FJD"],"funding":["NIAID NIH HHS","Medical Research Council","National Institutes of Health","National Institute of General Medical Sciences","Wellcome Trust","NIH HHS","NIGMS NIH HHS","National Science Foundation","MRC"],"pagination":["e1701264"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5600524"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["3(9)"],"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."],"journal":["Science advances"],"pubmed_title":["CryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction."],"pmcid":["PMC5600524"],"funding_grant_id":["GM085043","MC_UP_A025_1013","award338731","AI039394","GM104601","R01 AI039394","award338730","OD019995","ACI-1238993","S10 OD019995","award341008","206422/Z/17/Z","OCI 07-25070","P41 GM104601","R01 GM085043","award338728","award338729","award338726","award338727","award338724","award338725","GM067887","P50 GM082251","R01 GM067887","award325635","R37 AI039394","U24 GM116790"],"pubmed_authors":["Alvarez FJD","Scheres SHW","He S","Perilla JR","Jang S","Engelman AN","Schulten K","Zhang P"],"additional_accession":[]},"is_claimable":false,"name":"CryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction.","description":"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.","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Sep","modification":"2024-02-16T09:42:06.822Z","creation":"2019-03-27T02:56:32Z"},"accession":"S-EPMC5600524","cross_references":{"pubmed":["28929138"],"doi":["10.1126/sciadv.1701264"]}}