4JN4
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
4JN4 の概要
| エントリーDOI | 10.2210/pdb4jn4/pdb |
| 分子名称 | Chaperone protein DnaK, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
| 機能のキーワード | dnak, chaperone, 70kda heat shock protein (hsp70), single-wavelength anomalous diffraction (sad), native structure determination, multiple crystals |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Cytoplasm: P0A6Y8 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 134274.73 |
| 構造登録者 | Qi, R.,Sarbeng, E.B.,Liu, Q.,Le, K.Q.,Xu, X.,Xu, H.,Yang, J.,Wong, J.L.,Vorvis, C.,Hendrickson, W.A.,Zhou, L.,Liu, Q. (登録日: 2013-03-14, 公開日: 2013-05-29, 最終更新日: 2024-02-28) |
| 主引用文献 | Qi, R.,Sarbeng, E.B.,Liu, Q.,Le, K.Q.,Xu, X.,Xu, H.,Yang, J.,Wong, J.L.,Vorvis, C.,Hendrickson, W.A.,Zhou, L.,Liu, Q. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP. Nat.Struct.Mol.Biol., 20:900-907, 2013 Cited by PubMed Abstract: The 70-kilodalton (kDa) heat-shock proteins (Hsp70s) are ubiquitous molecular chaperones essential for cellular protein folding and proteostasis. Each Hsp70 has two functional domains: a nucleotide-binding domain (NBD), which binds and hydrolyzes ATP, and a substrate-binding domain (SBD), which binds extended polypeptides. NBD and SBD interact little when in the presence of ADP; however, ATP binding allosterically couples the polypeptide- and ATP-binding sites. ATP binding promotes polypeptide release; polypeptide rebinding stimulates ATP hydrolysis. This allosteric coupling is poorly understood. Here we present the crystal structure of an intact ATP-bound Hsp70 from Escherichia coli at 1.96-Å resolution. The ATP-bound NBD adopts a unique conformation, forming extensive interfaces with an SBD that has changed radically, having its α-helical lid displaced and the polypeptide-binding channel of its β-subdomain restructured. These conformational changes, together with our biochemical assays, provide a structural explanation for allosteric coupling in Hsp70 activity. PubMed: 23708608DOI: 10.1038/nsmb.2583 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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