4U6U

Crystal Structure of the Cog5-Cog7 complex from Kluyveromyces lactis

4U6U の概要

• エントリーDOI: 10.2210/pdb4u6u/pdb
• 分子名称: Cog7, Cog5 (2 entities in total)
• 機能のキーワード: multisubunit tethering complex, conserved oligomeric golgi complex, coiled coil, vesicle fusion, transport protein
• 由来する生物種: Kluyveromyces lactis (Yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 82698.30

構造登録者

Ha, J.Y.,Jeffrey, P.D.,Hughson, F.M. (登録日: 2014-07-29, 公開日: 2014-10-22, 最終更新日: 2023-12-27)

主引用文献

Ha, J.Y.,Pokrovskaya, I.D.,Climer, L.K.,Shimamura, G.R.,Kudlyk, T.,Jeffrey, P.D.,Lupashin, V.V.,Hughson, F.M.
Cog5-Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex.
Proc.Natl.Acad.Sci.USA, 111:15762-15767, 2014

PubMed Abstract: The conserved oligomeric Golgi (COG) complex is required, along with SNARE and Sec1/Munc18 (SM) proteins, for vesicle docking and fusion at the Golgi. COG, like other multisubunit tethering complexes (MTCs), is thought to function as a scaffold and/or chaperone to direct the assembly of productive SNARE complexes at the sites of membrane fusion. Reflecting this essential role, mutations in the COG complex can cause congenital disorders of glycosylation. A deeper understanding of COG function and dysfunction will likely depend on elucidating its molecular structure. Despite some progress toward this goal, including EM studies of COG lobe A (subunits 1-4) and higher-resolution structures of portions of Cog2 and Cog4, the structures of COG's eight subunits and the principles governing their assembly are mostly unknown. Here, we report the crystal structure of a complex between two lobe B subunits, Cog5 and Cog7. The structure reveals that Cog5 is a member of the complexes associated with tethering containing helical rods (CATCHR) fold family, with homology to subunits of other MTCs including the Dsl1, exocyst, and Golgi-associated retrograde protein (GARP) complexes. The Cog5-Cog7 interaction is analyzed in relation to the Dsl1 complex, the only other CATCHR-family MTC for which subunit interactions have been characterized in detail. Biochemical and functional studies validate the physiological relevance of the observed Cog5-Cog7 interface, indicate that it is conserved from yeast to humans, and demonstrate that its disruption in human cells causes defects in trafficking and glycosylation.

PubMed: 25331899
DOI: 10.1073/pnas.1414829111

実験手法

X-RAY DIFFRACTION (3 Å)