4XCD

Crystal structure of an octadecameric TF55 complex from S. solfataricus

4XCD の概要

• エントリーDOI: 10.2210/pdb4xcd/pdb
• 分子名称: Thermosome subunit beta, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: protein folding, thermosomes, chaperonin, chaperone
• 由来する生物種: Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 372786.36

構造登録者

Chaston, J.J.,Stewart, A.G.,Smits, C.,Stock, D. (登録日: 2014-12-17, 公開日: 2016-02-10, 最終更新日: 2023-09-27)

主引用文献

Chaston, J.J.,Smits, C.,Aragao, D.,Wong, A.S.,Ahsan, B.,Sandin, S.,Molugu, S.K.,Molugu, S.K.,Bernal, R.A.,Stock, D.,Stewart, A.G.
Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins.
Structure, 24:364-374, 2016

PubMed Abstract: Chaperonins are essential biological complexes assisting protein folding in all kingdoms of life. Whereas homooligomeric bacterial GroEL binds hydrophobic substrates non-specifically, the heterooligomeric eukaryotic CCT binds specifically to distinct classes of substrates. Sulfolobales, which survive in a wide range of temperatures, have evolved three different chaperonin subunits (α, β, γ) that form three distinct complexes tailored for different substrate classes at cold, normal, and elevated temperatures. The larger octadecameric β complexes cater for substrates under heat stress, whereas smaller hexadecameric αβ complexes prevail under normal conditions. The cold-shock complex contains all three subunits, consistent with greater substrate specificity. Structural analysis using crystallography and electron microscopy reveals the geometry of these complexes and shows a novel arrangement of the α and β subunits in the hexadecamer enabling incorporation of the γ subunit.

PubMed: 26853941
DOI: 10.1016/j.str.2015.12.016

実験手法

X-RAY DIFFRACTION (3.79 Å)