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Instruments / Technical Area	Publication Details	Published	Actions
Krios III-Titan Krios III at Diamond	Structural basis of TRAPPIII‐mediated Rab1 activation Aaron M. N. Joiner , Ben P. Phillips , Kumar Yugandhar , Ethan J Sanford , Marcus B Smolka , Haiyuan Yu , Elizabeth A. Miller , J Christopher Fromme The Embo Journal 74 DOI: 10.15252/embj.2020107607 Diamond Proposal Number(s): [17434] Open Access Show Abstract ▼ Abstract: The GTPase Rab1 is a master regulator of the early secretory pathway and is critical for autophagy. Rab1 activation is controlled by its guanine nucleotide exchange factor, the multisubunit TRAPPIII complex. Here, we report the 3.7 Å cryo-EM structure of the Saccharomyces cerevisiae TRAPPIII complex bound to its substrate Rab1/Ypt1. The structure reveals the binding site for the Rab1/Ypt1 hypervariable domain, leading to a model for how the complex interacts with membranes during the activation reaction. We determined that stable membrane binding by the TRAPPIII complex is required for robust activation of Rab1/Ypt1 in vitro and in vivo, and is mediated by a conserved amphipathic α-helix within the regulatory Trs85 subunit. Our results show that the Trs85 subunit serves as a membrane anchor, via its amphipathic helix, for the entire TRAPPIII complex. These findings provide a structural understanding of Rab activation on organelle and vesicle membranes.	May 2021
I03-Macromolecular Crystallography I23-Long wavelength MX Krios III-Titan Krios III at Diamond	The architecture of EMC reveals a path for membrane protein insertion John P. O'Donnell , Ben P. Phillips , Yuichi Yagita , Szymon Juszkiewicz , Armin Wagner , Duccio Malinverni , Robert J Keenan , Elizabeth Miller , Ramanujan S. Hegde Elife 9 DOI: 10.7554/eLife.57887 Diamond Proposal Number(s): [21426] Open Access Show Abstract ▼ Abstract: Approximately 25% of eukaryotic genes code for integral membrane proteins that are assembled at the endoplasmic reticulum. An abundant and widely conserved multi-protein complex termed EMC has been implicated in membrane protein biogenesis, but its mechanism of action is poorly understood. Here, we define the composition and architecture of human EMC using biochemical assays, crystallography of individual subunits, site-specific photocrosslinking, and cryo-EM reconstruction. Our results suggest that EMC's cytosolic domain contains a large, moderately hydrophobic vestibule that can bind a substrate's transmembrane domain (TMD). The cytosolic vestibule leads into a lumenally-sealed, lipid-exposed intramembrane groove large enough to accommodate a single substrate TMD. A gap between the cytosolic vestibule and intramembrane groove provides a potential path for substrate egress from EMC. These findings suggest how EMC facilitates energy-independent membrane insertion of TMDs, explain why only short lumenal domains are translocated by EMC, and constrain models of EMC's proposed chaperone function.	May 2020

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