4RV7

Characterization of an essential diadenylate cyclase

4RV7 の概要

• エントリーDOI: 10.2210/pdb4rv7/pdb
• 分子名称: Diadenylate cyclase, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: dac-fold, atp binding, c-di-amp binding, transferase
• 由来する生物種: Listeria monocytogenes EGD-e
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 86247.35

構造登録者

Dickmanns, A.,Neumann, P.,Ficner, R. (登録日: 2014-11-25, 公開日: 2015-01-28, 最終更新日: 2023-09-20)

主引用文献

Rosenberg, J.,Dickmanns, A.,Neumann, P.,Gunka, K.,Arens, J.,Kaever, V.,Stulke, J.,Ficner, R.,Commichau, F.M.
Structural and Biochemical Analysis of the Essential Diadenylate Cyclase CdaA from Listeria monocytogenes.
J.Biol.Chem., 290:6596-6606, 2015

PubMed Abstract: The recently identified second messenger cyclic di-AMP (c-di-AMP) is involved in several important cellular processes, such as cell wall metabolism, maintenance of DNA integrity, ion transport, transcription regulation, and allosteric regulation of enzyme function. Interestingly, c-di-AMP is essential for growth of the Gram-positive model bacterium Bacillus subtilis. Although the genome of B. subtilis encodes three c-di-AMP-producing diadenlyate cyclases that can functionally replace each other, the phylogenetically related human pathogens like Listeria monocytogenes and Staphylococcus aureus possess only one enzyme, the diadenlyate cyclase CdaA. Because CdaA is also essential for growth of these bacteria, the enzyme is a promising target for the development of novel antibiotics. Here we present the first crystal structure of the L. monocytogenes CdaA diadenylate cyclase domain that is conserved in many human pathogens. Moreover, biochemical characterization of the cyclase revealed an unusual metal cofactor requirement.

PubMed: 25605729
DOI: 10.1074/jbc.M114.630418

実験手法

X-RAY DIFFRACTION (2.8 Å)