3TY8

Crystal Structure of C. Thermocellum PNKP Ligase Domain Apo Form

3TY8 の概要

• エントリーDOI: 10.2210/pdb3ty8/pdb
• 関連するPDBエントリー: 3TY5 3TY9
• 分子名称: Polynucleotide 2',3'-cyclic phosphate phosphodiesterase / polynucleotide 5'-hydroxyl-kinase / polynucleotide 3'-phosphatase, GLYCEROL, D(-)-TARTARIC ACID, ... (4 entities in total)
• 機能のキーワード: dna ligase/mrna capping enzyme, rna ligase, adenylyltransferase, hen1, transferase
• 由来する生物種: Clostridium thermocellum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95671.10

構造登録者

Smith, P.,Wang, L.,Shuman, S. (登録日: 2011-09-23, 公開日: 2012-01-25, 最終更新日: 2023-09-13)

主引用文献

Smith, P.,Wang, L.K.,Nair, P.A.,Shuman, S.
The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.
Proc.Natl.Acad.Sci.USA, 109:2296-2301, 2012

PubMed Abstract: Pnkp is the end-healing and end-sealing component of an RNA repair system present in diverse bacteria from ten different phyla. To gain insight to the mechanism and evolution of this repair system, we determined the crystal structures of the ligase domain of Clostridium thermocellum Pnkp in three functional states along the reaction pathway: apoenzyme, ligase • ATP substrate complex, and covalent ligase-AMP intermediate. The tertiary structure is composed of a classical ligase nucleotidyltransferase module that is embellished by a unique α-helical insert module and a unique C-terminal α-helical module. Structure-guided mutational analysis identified active site residues essential for ligase adenylylation. Pnkp defines a new RNA ligase family with signature structural and functional properties.

PubMed: 22308407
DOI: 10.1073/pnas.1116827109

実験手法

X-RAY DIFFRACTION (2.6 Å)