6A4F

Separated uridine bound Oligoribonuclease (ORN) from Colwellia psychrerythraea strain 34H

6A4F の概要

• エントリーDOI: 10.2210/pdb6a4f/pdb
• 分子名称: Oligoribonuclease, URIDINE-5'-MONOPHOSPHATE, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: oligoribonuclease, exonuclease, colwellia psychrerythraea strain 34h, hydrolase
• 由来する生物種: Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43190.23

構造登録者

Lee, C.W.,Park, S.,Lee, J.H. (登録日: 2018-06-19, 公開日: 2019-03-13, 最終更新日: 2024-03-27)

主引用文献

Lee, C.W.,Park, S.H.,Jeong, C.S.,Cha, S.S.,Park, H.,Lee, J.H.
Structural basis of small RNA hydrolysis by oligoribonuclease (CpsORN) from Colwellia psychrerythraea strain 34H.
Sci Rep, 9:2649-2649, 2019

PubMed Abstract: Cells regulate their intracellular mRNA levels by using specific ribonucleases. Oligoribonuclease (ORN) is a 3'-5' exoribonuclease for small RNA molecules, important in RNA degradation and re-utilisation. However, there is no structural information on the ligand-binding form of ORNs. In this study, the crystal structures of oligoribonuclease from Colwellia psychrerythraea strain 34H (CpsORN) were determined in four different forms: unliganded-structure, thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP)-bound, two separated uridine-bound, and two linked uridine (U-U)-bound forms. The crystal structures show that CpsORN is a tight dimer, with two separated active sites and one divalent metal cation ion in each active site. These structures represent several snapshots of the enzymatic reaction process, which allowed us to suggest a possible one-metal-dependent reaction mechanism for CpsORN. Moreover, the biochemical data support our suggested mechanism and identified the key residues responsible for enzymatic catalysis of CpsORN.

PubMed: 30804410
DOI: 10.1038/s41598-019-39641-0

実験手法

X-RAY DIFFRACTION (2.21 Å)