1JVT

CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE FORM)

1JVT の概要

• エントリーDOI: 10.2210/pdb1jvt/pdb
• 関連するPDBエントリー: 1JVU 1JVV
• 分子名称: RIBONUCLEASE A (2 entities in total)
• 機能のキーワード: protein dynamics, protein structure-function, 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: 2
• 化学式量合計: 27416.65

構造登録者

Vitagliano, L.,Merlino, A.,Zagari, A.,Mazzarella, L. (登録日: 2001-08-31, 公開日: 2002-06-05, 最終更新日: 2024-10-09)

主引用文献

Vitagliano, L.,Merlino, A.,Zagari, A.,Mazzarella, L.
Reversible Substrate-Induced Domain Motions in Ribonuclease A
Proteins, 46:97-104, 2002

PubMed Abstract: Despite the increasing number of successful determinations of complex protein structures the understanding of their dynamics properties is still rather limited. Using X-ray crystallography, we demonstrate that ribonuclease A (RNase A) undergoes significant domain motions upon ligand binding. In particular, when cytidine 2'-monophosphate binds to RNase A, the structure of the enzyme becomes more compact. Interestingly, our data also show that these structural alterations are fully reversible in the crystal state. These findings provide structural bases for the dynamic behavior of RNase A in the binding of the substrate shown by Petsko and coworkers (Rasmussen et al. Nature 1992;357:423-424). These subtle domain motions may assume functional relevance for more complex system and may play a significant role in the cooperativity of oligomeric enzymes.

PubMed: 11746706
DOI: 10.1002/prot.10033

実験手法

X-RAY DIFFRACTION (2.05 Å)