4XJ5
Crystal structure of Vibrio cholerae DncV 3'-deoxy GTP bound form
Summary for 4XJ5
| Entry DOI | 10.2210/pdb4xj5/pdb |
| Related | 4XJ1 4XJ3 4XJ4 4XJ6 |
| Descriptor | Cyclic AMP-GMP synthase, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | cyclic gmp-amp synthase, bacterial virulence, nucleotidyltransferase, transferase |
| Biological source | Vibrio cholerae O1 biovar El Tor str. N16961 More |
| Total number of polymer chains | 1 |
| Total formula weight | 46020.21 |
| Authors | Kato, K.,Ishii, R.,Ishitani, R.,Nureki, O. (deposition date: 2015-01-08, release date: 2015-04-29, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 25865248DOI: 10.1016/j.str.2015.01.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.552 Å) |
Structure validation
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