2KSQ

The myristoylated yeast ARF1 in a GTP and bicelle bound conformation

Summary for 2KSQ

• Entry DOI: 10.2210/pdb2ksq/pdb
• Descriptor: ADP-ribosylation factor 1, S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: arf, myristoylated, myristoyl, gtp, bicelle, er-golgi transport, golgi apparatus, gtp-binding, lipoprotein, myristate, nucleotide-binding, protein transport, transport, transport protein
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Golgi apparatus: P11076
• Total number of polymer chains: 1
• Total formula weight: 22360.67

Authors

Liu, Y.,Kahn, R.,Prestegard, J. (deposition date: 2010-01-12, release date: 2010-07-07, Last modification date: 2025-03-26)

Primary citation

Liu, Y.,Kahn, R.A.,Prestegard, J.H.
Dynamic structure of membrane-anchored Arf*GTP.
Nat.Struct.Mol.Biol., 17:876-881, 2010

PubMed Abstract: ADP ribosylation factors (Arfs) are N-myristoylated GTP/GDP switch proteins that have 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 nonmyristoylated 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.

PubMed: 20601958
DOI: 10.1038/nsmb.1853

Experimental method

SOLUTION NMR