6ZXB

Diguanylate cyclase DgcR (I-site mutant) in native state

6ZXB の概要

• エントリーDOI: 10.2210/pdb6zxb/pdb
• 分子名称: Putative GGDEF/response regulator receiver domain protein, 3'-DEOXY-GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: ggdef domain, receiver domain, rec, c-di-gmp, leptospira, signaling protein
• 由来する生物種: Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)'
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68258.52

構造登録者

Teixeira, R.D.,Schirmer, T. (登録日: 2020-07-29, 公開日: 2021-03-31, 最終更新日: 2024-01-31)

主引用文献

Teixeira, R.D.,Holzschuh, F.,Schirmer, T.
Activation mechanism of a small prototypic Rec-GGDEF diguanylate cyclase.
Nat Commun, 12:2162-2162, 2021

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: 33846343
DOI: 10.1038/s41467-021-22492-7

実験手法

X-RAY DIFFRACTION (2.2 Å)