6HVM

Structural characterization of CdaA-APO

6HVM の概要

• エントリーDOI: 10.2210/pdb6hvm/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: Diadenylate cyclase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: di-adenylate cyclase, second messenger, complex, c-di-amp, amp, transferase
• 由来する生物種: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39115.95

構造登録者

Heidemann, J.L.,Neumann, P.,Ficner, R. (登録日: 2018-10-11, 公開日: 2019-06-05, 最終更新日: 2024-05-15)

主引用文献

Heidemann, J.L.,Neumann, P.,Dickmanns, A.,Ficner, R.
Crystal structures of the c-di-AMP-synthesizing enzyme CdaA.
J.Biol.Chem., 294:10463-10470, 2019

PubMed Abstract: Cyclic di-AMP (c-di-AMP) is the only second messenger known to be essential for bacterial growth. It has been found mainly in Gram-positive bacteria, including pathogenic bacteria like CdaA is the sole diadenylate cyclase in , making this enzyme an attractive target for the development of novel antibiotic compounds. Here we report crystal structures of CdaA from in the apo state, in the post-catalytic state with bound c-di-AMP and catalytic Co ions, as well as in a complex with AMP. These structures reveal the flexibility of a tyrosine side chain involved in locking the adenine ring after ATP binding. The essential role of this tyrosine was confirmed by mutation to Ala, leading to drastic loss of enzymatic activity.

PubMed: 31118276
DOI: 10.1074/jbc.RA119.009246

実験手法

X-RAY DIFFRACTION (2 Å)