3SZ7

Crystal structure of the Sgt2 TPR domain from Aspergillus fumigatus

3SZ7 の概要

• エントリーDOI: 10.2210/pdb3sz7/pdb
• 分子名称: Hsc70 cochaperone (SGT) (2 entities in total)
• 機能のキーワード: tpr domain, cochaperone, get4, get5, get3, mdy2, ssa1, sse1, hsp104, hsc82, chaperone regulator
• 由来する生物種: Aspergillus fumigatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17268.11

構造登録者

Chartron, J.W.,Gonzalez, G.M.,Clemons Jr., W.M. (登録日: 2011-07-18, 公開日: 2011-08-10, 最終更新日: 2023-09-13)

主引用文献

Chartron, J.W.,Gonzalez, G.M.,Clemons, W.M.
A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex.
J.Biol.Chem., 286:34325-34334, 2011

PubMed Abstract: The insertion of tail-anchored transmembrane (TA) proteins into the appropriate membrane is a post-translational event that requires stabilization of the transmembrane domain and targeting to the proper destination. Sgt2 is a heat-shock protein cognate (HSC) co-chaperone that preferentially binds endoplasmic reticulum-destined TA proteins and directs them to the GET pathway via Get4 and Get5. Here, we present the crystal structure from a fungal Sgt2 homolog of the tetratrico-repeat (TPR) domain and part of the linker that connects to the C-terminal domain. The linker extends into the two-carboxylate clamp of the TPR domain from a symmetry-related molecule mimicking the binding to HSCs. Based on this structure, we provide biochemical evidence that the Sgt2 TPR domain has the ability to directly bind multiple HSC family members. The structure allows us to propose features involved in this lower specificity relative to other TPR containing co-chaperones. We further show that a dimer of Sgt2 binds a single Get5 and use small angle x-ray scattering to characterize the domain arrangement of Sgt2 in solution. These results allow us to present a structural model of the Sgt2-Get4/Get5-HSC complex.

PubMed: 21832041
DOI: 10.1074/jbc.M111.277798

実験手法

X-RAY DIFFRACTION (1.72 Å)