4GOE

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

4GOE の概要

• エントリーDOI: 10.2210/pdb4goe/pdb
• 関連するPDBエントリー: 4GOC 4GOD 4GOF
• 分子名称: Small glutamine-rich tetratricopeptide repeat-containing protein alpha, BETA-MERCAPTOETHANOL, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: four-helix bundle, protein-protein interaction, ubl4a ubiquitin-like domain, protein binding
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11590.60

構造登録者

Chartron, J.W.,VanderVelde, D.G.,Clemons Jr., W.M. (登録日: 2012-08-19, 公開日: 2012-11-21, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.45 Å)