6HVM

Structural characterization of CdaA-APO

Summary for 6HVM

• Entry DOI: 10.2210/pdb6hvm/pdb
• Related PRD ID: PRD_900003
• Descriptor: Diadenylate cyclase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: di-adenylate cyclase, second messenger, complex, c-di-amp, amp, transferase
• Biological source: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
• Total number of polymer chains: 2
• Total formula weight: 39115.95

Authors

Heidemann, J.L.,Neumann, P.,Ficner, R. (deposition date: 2018-10-11, release date: 2019-06-05, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)