3SZR
Crystal structure of modified nucleotide-free human MxA
Summary for 3SZR
| Entry DOI | 10.2210/pdb3szr/pdb |
| Related | 3LJB |
| Descriptor | Interferon-induced GTP-binding protein Mx1 (1 entity in total) |
| Functional Keywords | interferon-induced antiviral gtpase, membrane associated, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 69176.81 |
| Authors | Gao, S.,Daumke, O. (deposition date: 2011-07-19, release date: 2011-10-12, Last modification date: 2023-09-13) |
| Primary citation | Gao, S.,von der Malsburg, A.,Dick, A.,Faelber, K.,Schroder, G.F.,Haller, O.,Kochs, G.,Daumke, O. Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function. Immunity, 35:514-525, 2011 Cited by PubMed Abstract: Human myxovirus resistance protein 1 (MxA) is an interferon-induced dynamin-like GTPase that acts as a cell-autonomous host restriction factor against many viral pathogens including influenza viruses. To study the molecular principles of its antiviral activity, we determined the crystal structure of nucleotide-free MxA, which showed an extended three-domain architecture. The central bundle signaling element (BSE) connected the amino-terminal GTPase domain with the stalk via two hinge regions. MxA oligomerized in the crystal via the stalk and the BSE, which in turn interacted with the stalk of the neighboring monomer. We demonstrated that the intra- and intermolecular domain interplay between the BSE and stalk was essential for oligomerization and the antiviral function of MxA. Based on these results, we propose a structural model for the mechano-chemical coupling in ring-like MxA oligomers as the principle mechanism for this unique antiviral effector protein. PubMed: 21962493DOI: 10.1016/j.immuni.2011.07.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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