2JQQ

Solution structure of Saccharomyces cerevisiae conserved oligomeric Golgi subunit 2 protein (Cog2p)

2JQQ の概要

• エントリーDOI: 10.2210/pdb2jqq/pdb
• NMR情報: BMRB: 15290
• 分子名称: Conserved oligomeric Golgi complex subunit 2 (1 entity in total)
• 機能のキーワード: protein, helical bundle, vesicular transport, tethering, protein transport
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23442.50

構造登録者

Cavanaugh, L.F.,Chen, X.,Pelczer, I.,Rizo, J.,Hughson, F.M. (登録日: 2007-06-06, 公開日: 2007-06-19, 最終更新日: 2024-05-08)

主引用文献

Cavanaugh, L.F.,Chen, X.,Richardson, B.C.,Ungar, D.,Pelczer, I.,Rizo, J.,Hughson, F.M.
Structural analysis of conserved oligomeric Golgi complex subunit 2
J.Biol.Chem., 282:23418-23426, 2007

PubMed Abstract: The conserved oligomeric Golgi (COG) complex is strongly implicated in retrograde vesicular trafficking within the Golgi apparatus. Although its mechanism of action is poorly understood, it has been proposed to function by mediating the initial physical contact between transport vesicles and their membrane targets. An analogous role in tethering vesicles has been suggested for at least six additional large multisubunit complexes, including the exocyst, a complex essential for trafficking to the plasma membrane. Here we report the solution structure of a large portion of yeast Cog2p, one of eight subunits composing the COG complex. The structure reveals a six-helix bundle with few conserved surface features but a general resemblance to recently determined crystal structures of four different exocyst subunits. This finding provides the first structural evidence that COG, like the exocyst and potentially other tethering complexes, is constructed from helical bundles. These structures may represent platforms for interaction with other trafficking proteins including SNAREs (soluble N-ethylmaleimide factor attachment protein receptors) and Rabs.

PubMed: 17565980
DOI: 10.1074/jbc.M703716200

実験手法

SOLUTION NMR