4GOE

Crystal structure of the SGTA homodimerization domain with a covalent modification of a single C38

Summary for 4GOE

• Entry DOI: 10.2210/pdb4goe/pdb
• Related: 4GOC 4GOD 4GOF
• Descriptor: Small glutamine-rich tetratricopeptide repeat-containing protein alpha, BETA-MERCAPTOETHANOL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: four-helix bundle, protein-protein interaction, ubl4a ubiquitin-like domain, protein binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 11590.60

Authors

Chartron, J.W.,VanderVelde, D.G.,Clemons Jr., W.M. (deposition date: 2012-08-19, release date: 2012-11-21, Last modification date: 2024-03-13)

Primary citation

Chartron, J.W.,Vandervelde, D.G.,Clemons, W.M.
Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface.
Cell Rep, 2:1620-1632, 2012

PubMed Abstract: In the cytoplasm, the correct delivery of membrane proteins is an essential and highly regulated process. The posttranslational targeting of the important tail-anchor membrane (TA) proteins has recently been under intense investigation. A specialized pathway, called the guided entry of TA proteins (GET) pathway in yeast and the transmembrane domain recognition complex (TRC) pathway in vertebrates, recognizes endoplasmic-reticulum-targeted TA proteins and delivers them through a complex series of handoffs. An early step is the formation of a complex between Sgt2/SGTA, a cochaperone with a presumed ubiquitin-like-binding domain (UBD), and Get5/UBL4A, a ubiquitin-like domain (UBL)-containing protein. We structurally characterize this UBD/UBL interaction for both yeast and human proteins. This characterization is supported by biophysical studies that demonstrate that complex formation is mediated by electrostatics, generating an interface that has high-affinity with rapid kinetics. In total, this work provides a refined model of the interplay of Sgt2 homologs in TA targeting.

PubMed: 23142665
DOI: 10.1016/j.celrep.2012.10.010

Experimental method

X-RAY DIFFRACTION (1.45 Å)