Dynamiting Viruses with MxA Anthony J. Sadler, Bryan R.G. Williams  Immunity  Volume 35, Issue 4, Pages 491-493 (October 2011) DOI: 10.1016/j.immuni.2011.10.005 Copyright © 2011 Elsevier Inc. Terms and Conditions

Figure 1 Oligomerization, GTP Binding, Hydrolysis, and Conformational Changes in MxA Monomeric MxA consists of the globular G, BSE, and GED domains that coordinate oligomerization to form higher-order structures and impart mechanical movement to the macromolecule. Oligomerization proceeds by interactions between the GED and BSE to form protein bilayers that form into ring-shaped structures that have the G domains pointed outward and the substrate interaction domains pointed inwards. Separate MxA ring structures initially interact weakly via their G domains, thereby breaking the BSE-stalk inhibition of the enzyme's GTPase activity. Subsequent binding and hydrolysis of GTP causes intramolecular movement that probably generates a twisting motion of separate MxA rings relative to each other. Presumably this twisting motion imparts critical sheer stress to viral nucleoproteins bound at the internal surface of the MxA ring. Immunity 2011 35, 491-493DOI: (10.1016/j.immuni.2011.10.005) Copyright © 2011 Elsevier Inc. Terms and Conditions