- PDB-4xci: Crystal structure of a hexadecameric TF55 complex from S. solfata... -
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基本情報
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データベース: PDB / ID: 4xci
タイトル
Crystal structure of a hexadecameric TF55 complex from S. solfataricus, crystal form II
要素
Thermosome subunit alpha
Thermosome subunit beta
キーワード
CHAPERONE / Protein Folding / Thermosomes / Chaperonin
機能・相同性
機能・相同性情報
chaperonin-containing T-complex / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / ATP hydrolysis activity / ATP binding / identical protein binding 類似検索 - 分子機能
ジャーナル: Structure / 年: 2016 タイトル: Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins. 著者: Jessica J Chaston / Callum Smits / David Aragão / Andrew S W Wong / Bilal Ahsan / Sara Sandin / Sudheer K Molugu / Sanjay K Molugu / Ricardo A Bernal / Daniela Stock / Alastair G Stewart / 要旨: Chaperonins are essential biological complexes assisting protein folding in all kingdoms of life. Whereas homooligomeric bacterial GroEL binds hydrophobic substrates non-specifically, the ...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.