Dynamic structure of membrane-anchored Arf*GTP

• Type of Material: Article
• Authors: Yizhou Liu, University of Georgia; Richard A Kahn, Emory University; James H. Prestegard, University of Georgia
• Language: English
• Date: 2010-07
• Publisher: Nature Publishing Group
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2010 Nature America, Inc. All rights reserved.
• Final Published Version (URL): http://www.nature.com/nsmb/journal/v17/n7/full/nsmb.1853.html
• Title of Journal or Parent Work: Nature Structural & Molecular Biology
• ISSN: 1545-9993
• Volume: 17
• Issue: 7
• Start Page: 876
• End Page: 881
• Grant/Funding Information: This work was supported by a grant from the National Institutes of Health (GM61268).
• Research Categories: Chemistry, Biochemistry; Biology, Molecular

Abstract

Arfs (ADP ribosylation factors) are N-myristoylated GTP/GDP switch proteins playing key regulatory roles in vesicle transport in eukaryotic cells. ARFs execute their roles by anchoring to membrane surfaces where they interact with other proteins to initiate budding and maturation of transport vesicles. However, existing structures of Arf•GTP are limited to non-myristoylated and truncated forms with impaired membrane binding. We report a high resolution NMR structure for full-length myristoylated yeast (Saccharomyces cerevisiae) Arf1 in complex with a membrane mimic. The two domain structure, in which the myristoylated N-terminal helix is separated from the C-terminal domain by a flexible linker, suggests a level of adaptability in binding modes for the myriad of proteins with which Arf interacts, and allows predictions of specific lipid binding sites on some of these proteins.