4XJ6

Crystal structure of Escherichia coli DncV 3'-deoxy GTP bound form

4XJ6 の概要

• エントリーDOI: 10.2210/pdb4xj6/pdb
• 関連するPDBエントリー: 4XJ1 4XJ3 4XJ4 4XJ5
• 分子名称: VC0179-like protein, MAGNESIUM ION, 3'-DEOXY-GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: cyclic gmp-amp synthase, bacterial virulence, nucleotidyltransferase, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47879.80

構造登録者

Kato, K.,Ishii, R.,Ishitani, R.,Nureki, O. (登録日: 2015-01-08, 公開日: 2015-04-29, 最終更新日: 2024-03-20)

主引用文献

Kato, K.,Ishii, R.,Hirano, S.,Ishitani, R.,Nureki, O.
Structural Basis for the Catalytic Mechanism of DncV, Bacterial Homolog of Cyclic GMP-AMP Synthase
Structure, 23:843-850, 2015

PubMed Abstract: Cyclic dinucleotides (CDNs) play key roles as second messengers and signaling molecules in bacteria and metazoans. The newly identified dinucleotide cyclase in Vibrio cholerae (DncV) produces three different CDNs containing two 3'-5' phosphodiester bonds, and its predominant product is cyclic GMP-AMP, whereas mammalian cyclic GMP-AMP synthase (cGAS) produces only cyclic GMP-AMP containing mixed 2'-5' phosphodiester bonds. We report the crystal structures of V. cholerae and Escherichia coli DncV in complex with various nucleotides in the pre-reaction states. The high-resolution structures revealed that DncV preferably recognizes ATP and GTP as acceptor and donor nucleotides, respectively, in the first nucleotidyl transfer reaction. Considering the recently reported intermediate structures, our pre-reaction state structures provide the precise mechanism of 3'-5' linked cyclic AMP-GMP production in bacteria. A comparison with cGAS in the pre-reaction states suggests that the orientation of the acceptor nucleotide primarily determines the distinct linkage specificities between DncV and cGAS.

PubMed: 25865248
DOI: 10.1016/j.str.2015.01.023

実験手法

X-RAY DIFFRACTION (2.31 Å)