7RWK

Structure of Cap5 from Asticcacaulis sp.

Summary for 7RWK

• Entry DOI: 10.2210/pdb7rwk/pdb
• Descriptor: SAVED domain-containing protein, ZINC ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: dna nuclease saved sensor effector, unknown function
• Biological source: Asticcacaulis sp. YBE204
• Total number of polymer chains: 2
• Total formula weight: 87050.39

Authors

Huang, R.H.,Fatma, S.,Chakravarti, A. (deposition date: 2021-08-20, release date: 2021-11-10, Last modification date: 2024-05-22)

Primary citation

Fatma, S.,Chakravarti, A.,Zeng, X.,Huang, R.H.
Molecular mechanisms of the CdnG-Cap5 antiphage defense system employing 3',2'-cGAMP as the second messenger.
Nat Commun, 12:6381-6381, 2021

PubMed Abstract: Cyclic-oligonucleotide-based antiphage signaling systems (CBASS) are diverse and abundant in bacteria. Here, we present the biochemical and structural characterization of two CBASS systems, composed of CdnG and Cap5, from Asticcacaulis sp. and Lactococcus lactis. We show that CdnG from Asticcacaulis sp. synthesizes 3',2'-cGAMP in vitro, and 3',2'-cGAMP is the biological signaling molecule that activates Cap5 for DNA degradation. Crystal structures of Cap5, together with the SAVED domain in complex with 3',2'-cGAMP, provide insight into the architecture of Cap5 as well as molecular recognition of 3',2'-cGAMP by the SAVED domain of Cap5. Amino acid conservation of the SAVED domain of Cap5, together with mutational studies, led us to propose a mechanism of Back-to-Front stacking of two SAVED domains, mediated by 3',2'-cGAMP, to activate HNH nuclease domain for DNA degradation. This study of the most abundant CBASS system provides insights into the mechanisms employed by bacteria in their conflicts against phage.

PubMed: 34737303
DOI: 10.1038/s41467-021-26738-2

Experimental method

X-RAY DIFFRACTION (2.39 Å)