Structural characterization by small angle scattering suggests models for monomeric and dimeric forms of full-length ezrin

Simple item page
dc.contributor.authorPhang, JMen_AU
dc.contributor.authorHarrop, SJen_AU
dc.contributor.authorDuff, APen_AU
dc.contributor.authorSokolova, AVen_AU
dc.contributor.authorCrossett, Ben_AU
dc.contributor.authorWalsh, JCen_AU
dc.contributor.authorBeckham, SAen_AU
dc.contributor.authorNguyen, CDen_AU
dc.contributor.authorDavies, RBen_AU
dc.contributor.authorGlöckner, Cen_AU
dc.contributor.authorBromley, EHen_AU
dc.contributor.authorWilk, KEen_AU
dc.contributor.authorCurmi, PMen_AU
dc.date.accessioned2021-10-26T23:09:38Zen_AU
dc.date.available2021-10-26T23:09:38Zen_AU
dc.date.issued2016-11-29en_AU
dc.date.statistics2021-10-12en_AU
dc.description.abstractEzrin is member of the ERM (Ezrin-Radixin-Moesin) family of proteins that have been conserved through metazoan evolution. These proteins have dormant and active forms, there the latter links the actin cytoskeleton to membranes. ERM proteins have three domains: an N-terminal FERM (band Four-point-one ERM) domain comprising three subdomains (F1, F2 and F3); a helical domain; and a C-terminal actin-binding domain. In the dormant form, FERM and C-terminal domains form a stable complex. We have determined crystal structures of the active FERM domain and the dormant FERM:C-terminal domain complex of human ezrin. We observe bistable array of phenylalanine residues in the core of subdomain F3 that is mobile in the active form and locked in the dormant form. As subdomain F3 is pivotal in binding membrane proteins and phospholipids, these transitions may facilitate activation and signaling. Full-length ezrin forms stable monomers and dimers. We used small-angle x-ray scattering to determine the solution structures of these species. As expected, the monomer shows a globular domain with a protruding helical coiled-coil. The dimer shows an elongated dumbbell structure that is twice as long as the monomer. By aligning ERM sequences spanning metazoan evolution, we show that the central helical region is conserved, preserving the heptad repeat. Using this, we have built a dimer model where each monomer forms half of an elongated anti-parallel coiled-coil with domain swapped FERM:C-terminal domain complexes at each end. The model suggests that ERM dimers may bind to actin in a parallel fashion.en_AU
dc.identifier.citationPhang, J. M., Harrop, S. J., Duff, A. P., Sokolova, A. V., Crossett, B., Walsh, J. C., Beckham, S. A., Nguyen, C. D., Davies, R. B., Glöckner, C., Bromley, E. H., Wilk, K. E., & Curmi, P. M. (2016). Structural characterization by small angle scattering suggests models for monomeric and dimeric forms of full-length ezrin. Paper presented at 13th AINSE-ANBUG Neutron Scattering Symposium, Sydney, NSW, Australia, 29-30 November 2016.en_AU
dc.identifier.conferenceenddate30 November 2016en_AU
dc.identifier.conferencename13th AINSE-ANBUG Neutron Scattering Symposiumen_AU
dc.identifier.conferenceplaceSydney, NSW, Australiaen_AU
dc.identifier.conferencestartdate29 November 2016en_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/12112en_AU
dc.language.isoenen_AU
dc.publisherAustralian Institute of Nuclear Science and Engineeringen_AU
dc.subjectProteinsen_AU
dc.subjectMembranesen_AU
dc.subjectCrystal structureen_AU
dc.subjectPhenylalanineen_AU
dc.subjectPhospholipidsen_AU
dc.subjectDimersen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectMonomersen_AU
dc.titleStructural characterization by small angle scattering suggests models for monomeric and dimeric forms of full-length ezrinen_AU
dc.typeConference Abstracten_AU
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Abstract_Handbook_v2(1).pdf
Size:
1.87 MB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.63 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Conference Publications