1TA8

Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal

1TA8 の概要

• エントリーDOI: 10.2210/pdb1ta8/pdb
• 分子名称: DNA ligase, NAD-dependent, SULFATE ION, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: nucleotidyl transferase fold, ligase
• 由来する生物種: Enterococcus faecalis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38605.10

構造登録者

Gajiwala, K.S.,Pinko, C. (登録日: 2004-05-19, 公開日: 2004-11-23, 最終更新日: 2024-10-30)

主引用文献

Gajiwala, K.S.,Pinko, C.
Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal.
STRUCTURE, 12:1449-1459, 2004

PubMed Abstract: DNA ligase is an enzyme important for DNA repair and replication. Eukaryotic genomes encode ligases requiring ATP as the cofactor; bacterial genomes encode NAD(+)-dependent ligase. This difference in substrate specificities and the essentiality of NAD(+)-dependent ligase for bacterial survival make NAD(+)-dependent ligase a good target for designing highly specific anti-infectives. Any such structure-guided effort would require the knowledge of the precise mechanism of NAD+ recognition by the enzyme. We report the principles of NAD+ recognition by presenting the synthesis of NAD+ from nicotinamide mononucleotide (NMN) and AMP, catalyzed by Enterococcus faecalis ligase within the crystal lattice. Unprecedented conformational change, required to reorient the two subdomains of the protein for the condensation to occur and to recognize NAD+, is captured in two structures obtained using the same protein crystal. Structural data and sequence analysis presented here confirms and extends prior functional studies of the ligase adenylation reaction.

PubMed: 15296738
DOI: 10.1016/j.str.2004.05.017

実験手法

X-RAY DIFFRACTION (1.8 Å)