2APQ

Crystal Structure of an Active Site Mutant of Bovine Pancreatic Ribonuclease A (H119A-RNase A) with a 10-Glutamine expansion in the C-terminal hinge-loop.

2APQ の概要

• エントリーDOI: 10.2210/pdb2apq/pdb
• 関連するPDBエントリー: 1fs3
• 分子名称: Ribonuclease, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: an active site mutant of rnase a (h119a) with an amyloidogenic expansion in the c-terminal hinge-loop region(between residues 112 and 113)., hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P61823
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15499.94

構造登録者

Sambashivan, S.,Liu, Y.,Sawaya, M.R.,Gingery, M.,Eisenberg, D. (登録日: 2005-08-16, 公開日: 2005-09-13, 最終更新日: 2024-10-16)

主引用文献

Sambashivan, S.,Liu, Y.,Sawaya, M.R.,Gingery, M.,Eisenberg, D.
Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.
Nature, 437:266-269, 2005

PubMed Abstract: Amyloid or amyloid-like fibrils are elongated, insoluble protein aggregates, formed in vivo in association with neurodegenerative diseases or in vitro from soluble native proteins, respectively. The underlying structure of the fibrillar or 'cross-beta' state has presented long-standing, fundamental puzzles of protein structure. These include whether fibril-forming proteins have two structurally distinct stable states, native and fibrillar, and whether all or only part of the native protein refolds as it converts to the fibrillar state. Here we show that a designed amyloid-like fibril of the well-characterized enzyme RNase A contains native-like molecules capable of enzymatic activity. In addition, these functional molecular units are formed from a core RNase A domain and a swapped complementary domain. These findings are consistent with the zipper-spine model in which a cross-beta spine is decorated with three-dimensional domain-swapped functional units, retaining native-like structure.

PubMed: 16148936
DOI: 10.1038/nature03916

実験手法

X-RAY DIFFRACTION (1.8 Å)