2LNZ

Solution structure of the Get5 carboxyl domain from S. cerevisiae

Summary for 2LNZ

• Entry DOI: 10.2210/pdb2lnz/pdb
• Related: 2LO0 3VEJ
• NMR Information: BMRB: 18186
• Descriptor: Ubiquitin-like protein MDY2 (1 entity in total)
• Functional Keywords: dimerization, homodimerization, protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm, cytosol: Q12285
• Total number of polymer chains: 2
• Total formula weight: 14247.78

Authors

Chartron, J.W.,Vandervelde, D.G.,Rao, M.,Clemons Jr., W.M. (deposition date: 2012-01-08, release date: 2012-01-25, Last modification date: 2024-05-15)

Primary citation

Chartron, J.W.,Vandervelde, D.G.,Rao, M.,Clemons, W.M.
Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex.
J.Biol.Chem., 287:8310-8317, 2012

PubMed Abstract: Tail-anchored trans-membrane proteins are targeted to membranes post-translationally. The proteins Get4 and Get5 form an obligate complex that catalyzes the transfer of tail-anchored proteins destined to the endoplasmic reticulum from Sgt2 to the cytosolic targeting factor Get3. Get5 forms a homodimer mediated by its carboxyl domain. We show here that a conserved motif exists within the carboxyl domain. A high resolution crystal structure and solution NMR structures of this motif reveal a novel and stable helical dimerization domain. We additionally determined a solution NMR structure of a divergent fungal homolog, and comparison of these structures allows annotation of specific stabilizing interactions. Using solution x-ray scattering and the structures of all folded domains, we present a model of the full-length Get4/Get5 complex.

PubMed: 22262836
DOI: 10.1074/jbc.M111.333252

Experimental method

SOLUTION NMR