8BA9 の概要
| エントリーDOI | 10.2210/pdb8ba9/pdb |
| EMDBエントリー | 15942 |
| 分子名称 | 60 kDa chaperonin, Co-chaperonin GroES, ALUMINUM FLUORIDE, ... (6 entities in total) |
| 機能のキーワード | groel, groes, chaperone |
| 由来する生物種 | Escherichia coli K-12 詳細 |
| タンパク質・核酸の鎖数 | 21 |
| 化学式量合計 | 853070.65 |
| 構造登録者 | |
| 主引用文献 | Gardner, S.,Darrow, M.C.,Lukoyanova, N.,Thalassinos, K.,Saibil, H.R. Structural basis of substrate progression through the bacterial chaperonin cycle. Proc Natl Acad Sci U S A, 120:e2308933120-, 2023 Cited by PubMed Abstract: The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM to determine structures of GroEL, GroEL-ADP·BeF, and GroEL-ADP·AlF-GroES all complexed with the model substrate Rubisco. Our structures provide a series of snapshots that show how the conformation and interactions of non-native Rubisco change as it proceeds through the GroEL-GroES reaction cycle. We observe specific charged and hydrophobic GroEL residues forming strong initial contacts with non-native Rubisco. Binding of ATP or ADP·BeF to GroEL-Rubisco results in the formation of an intermediate GroEL complex displaying striking asymmetry in the ATP/ADP·BeF-bound ring. In this ring, four GroEL subunits bind Rubisco and the other three are in the GroES-accepting conformation, suggesting how GroEL can recruit GroES without releasing bound substrate. Our cryoEM structures of stalled GroEL-ADP·AlF-Rubisco-GroES complexes show Rubisco folding intermediates interacting with GroEL-GroES via different sets of residues. PubMed: 38064510DOI: 10.1073/pnas.2308933120 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.7 Å) |
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