2K5U

Solution structure of myirstoylated yeast ARF1 protein, GDP-bound

2K5U の概要

• エントリーDOI: 10.2210/pdb2k5u/pdb
• 分子名称: ADP-ribosylation factor 1, GUANOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: arf, arf1, myristoyl, myrsitoylated, gdp, er-golgi transport, golgi apparatus, gtp-binding, lipoprotein, myristate, nucleotide-binding, protein transport, transport, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (rat)
• 細胞内の位置: Golgi apparatus: P11076
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21074.80

構造登録者

Prestegard, J.,Liu, Y. (登録日: 2008-06-30, 公開日: 2009-01-27, 最終更新日: 2022-03-16)

主引用文献

Liu, Y.,Kahn, R.A.,Prestegard, J.H.
Structure and Membrane Interaction of Myristoylated ARF1
Structure, 17:79-87, 2009

PubMed Abstract: ADP-ribosylation factors (ARFs) are small (21 kDa), monomeric GTPases that are important regulators of membrane traffic. When membrane bound, they recruit soluble adaptors to membranes and trigger the assembly of coating complexes involved in cargo selection and vesicular budding. N-myristoylation is a conserved feature of all ARF proteins that is required for its biological functions, although the mechanism(s) by which the myristate acts in ARF functions is not fully understood. Here we present the structure of a myristoylated ARF1 protein, determined by solution NMR methods, and an assessment of the influence of myristoylation on association of ARF1.GDP and ARF1.GTP with lipid bilayers. A model in which myristoylation contributes to both the regulation of guanine nucleotide exchange and stable membrane association is supported.

PubMed: 19141284
DOI: 10.1016/j.str.2008.10.020

実験手法

SOLUTION NMR