6ZXB
Diguanylate cyclase DgcR (I-site mutant) in native state
Summary for 6ZXB
| Entry DOI | 10.2210/pdb6zxb/pdb |
| Descriptor | Putative GGDEF/response regulator receiver domain protein, 3'-DEOXY-GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | ggdef domain, receiver domain, rec, c-di-gmp, leptospira, signaling protein |
| Biological source | Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)' |
| Total number of polymer chains | 2 |
| Total formula weight | 68258.52 |
| Authors | Teixeira, R.D.,Schirmer, T. (deposition date: 2020-07-29, release date: 2021-03-31, Last modification date: 2024-01-31) |
| Primary citation | Teixeira, R.D.,Holzschuh, F.,Schirmer, T. Activation mechanism of a small prototypic Rec-GGDEF diguanylate cyclase. Nat Commun, 12:2162-2162, 2021 Cited by PubMed Abstract: Diguanylate cyclases synthesising the bacterial second messenger c-di-GMP are found to be regulated by a variety of sensory input domains that control the activity of their catalytical GGDEF domain, but how activation proceeds mechanistically is, apart from a few examples, still largely unknown. As part of two-component systems, they are activated by cognate histidine kinases that phosphorylate their Rec input domains. DgcR from Leptospira biflexa is a constitutively dimeric prototype of this class of diguanylate cyclases. Full-length crystal structures reveal that BeF pseudo-phosphorylation induces a relative rotation of two rigid halves in the Rec domain. This is coupled to a reorganisation of the dimeric structure with concomitant switching of the coiled-coil linker to an alternative heptad register. Finally, the activated register allows the two substrate-loaded GGDEF domains, which are linked to the end of the coiled-coil via a localised hinge, to move into a catalytically competent dimeric arrangement. Bioinformatic analyses suggest that the binary register switch mechanism is utilised by many diguanylate cyclases with N-terminal coiled-coil linkers. PubMed: 33846343DOI: 10.1038/s41467-021-22492-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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