4CPG

Solution structure of the SGTA N-terminal domain

Summary for 4CPG

• Entry DOI: 10.2210/pdb4cpg/pdb
• NMR Information: BMRB: 19779
• Descriptor: SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN ALPHA (1 entity in total)
• Functional Keywords: chaperone, sgta, tail-anchored, get pathway, membrane protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm : O43765
• Total number of polymer chains: 2
• Total formula weight: 18486.52

Authors

Darby, J.F.,Krysztofinska, E.M.,Simpson, P.J.,Isaacson, R.L. (deposition date: 2014-02-06, release date: 2014-12-03, Last modification date: 2024-05-15)

Primary citation

Darby, J.F.,Krysztofinska, E.M.,Simpson, P.J.,Simon, A.C.,Leznicki, P.,Sriskandarajah, N.,Bishop, D.S.,Hale, L.R.,Alfano, C.,Conte, M.R.,Martinez-Lumbreras, S.,Thapaliya, A.,High, S.,Isaacson, R.L.
Solution Structure of the Sgta Dimerisation Domain and Investigation of its Interactions with the Ubiquitin-Like Domains of Bag6 and Ubl4A.
Plos One, 9:11328-, 2014

PubMed Abstract: The BAG6 complex resides in the cytosol and acts as a sorting point to target diverse hydrophobic protein substrates along their appropriate paths, including proteasomal degradation and ER membrane insertion. Composed of a trimeric complex of BAG6, TRC35 and UBL4A, the BAG6 complex is closely associated with SGTA, a co-chaperone from which it can obtain hydrophobic substrates.

PubMed: 25415308
DOI: 10.1371/JOURNAL.PONE.0113281

Experimental method

SOLUTION NMR