3HR0

Crystal structure of Homo sapiens Conserved Oligomeric Golgi subunit 4

Summary for 3HR0

• Entry DOI: 10.2210/pdb3hr0/pdb
• Descriptor: CoG4 (2 entities in total)
• Functional Keywords: conserved oligomeric golgi complex, intracellular trafficking, vesicle tethering, multisubunit tethering complex, exocyst, alternative splicing, golgi apparatus, membrane, phosphoprotein, protein transport, transport, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9H9E3
• Total number of polymer chains: 2
• Total formula weight: 59577.48

Authors

Richardson, B.C.,Ungar, D.,Nakamura, A.,Jeffrey, P.D.,Hughson, F.M. (deposition date: 2009-06-08, release date: 2009-07-21, Last modification date: 2024-02-21)

Primary citation

Richardson, B.C.,Smith, R.D.,Ungar, D.,Nakamura, A.,Jeffrey, P.D.,Lupashin, V.V.,Hughson, F.M.
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.
Proc.Natl.Acad.Sci.USA, 106:13329-13334, 2009

PubMed Abstract: The proper glycosylation of proteins trafficking through the Golgi apparatus depends upon the conserved oligomeric Golgi (COG) complex. Defects in COG can cause fatal congenital disorders of glycosylation (CDGs) in humans. The recent discovery of a form of CDG, caused in part by a COG4 missense mutation changing Arg 729 to Trp, prompted us to determine the 1.9 A crystal structure of a Cog4 C-terminal fragment. Arg 729 is found to occupy a key position at the center of a salt bridge network, thereby stabilizing Cog4's small C-terminal domain. Studies in HeLa cells reveal that this C-terminal domain, while not needed for the incorporation of Cog4 into COG complexes, is essential for the proper glycosylation of cell surface proteins. We also find that Cog4 bears a strong structural resemblance to exocyst and Dsl1p complex subunits. These complexes and others have been proposed to function by mediating the initial tethering between transport vesicles and their membrane targets; the emerging structural similarities provide strong evidence of a common evolutionary origin and may reflect shared mechanisms of action.

PubMed: 19651599
DOI: 10.1073/pnas.0901966106

Experimental method

X-RAY DIFFRACTION (1.9 Å)