5E86

isolated SBD of BiP with loop34 modification

5E86 の概要

• エントリーDOI: 10.2210/pdb5e86/pdb
• 関連するPDBエントリー: 5E84 5E85
• 分子名称: 78 kDa glucose-regulated protein (2 entities in total)
• 機能のキーワード: molecular chaperones;hsp70;bip;protein folding;endoplasmic reticulum;allosteric coupling, chaperone
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26029.45

構造登録者

Liu, Q.,Yang, J.,Nune, M.,Zong, Y.,Zhou, L. (登録日: 2015-10-13, 公開日: 2015-12-30, 最終更新日: 2024-03-06)

主引用文献

Yang, J.,Nune, M.,Zong, Y.,Zhou, L.,Liu, Q.
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
Structure, 23:2191-2203, 2015

PubMed Abstract: Binding immunoglobulin protein (BiP), an essential and ubiquitous Hsp70 chaperone in the ER, plays a key role in protein folding and quality control. BiP contains two functional domains: a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). NBD binds and hydrolyzes ATP; the substrates for SBD are extended polypeptides. ATP binding allosterically accelerates polypeptide binding and release. Although crucial to the chaperone activity, the molecular mechanisms of polypeptide binding and allosteric coupling of BiP are poorly understood. Here, we present crystal structures of an intact human BiP in the ATP-bound state, the first intact eukaryotic Hsp70 structure, and isolated BiP-SBD with a peptide substrate bound representing the ADP-bound state. These structures and our biochemical analysis demonstrate that BiP has a unique NBD-SBD interface that is highly conserved only in eukaryotic Hsp70s found in the cytosol and ER to fortify its ATP-bound state and promote the opening of its polypeptide-binding pocket.

PubMed: 26655470
DOI: 10.1016/j.str.2015.10.012

実験手法

X-RAY DIFFRACTION (2.681 Å)