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• W1433012466 abstract "This chapter begins with a discussion on a cyclic-di-GMP (c-di-GMP), a self-associating messenger molecule. The proteins involved in c-di-GMP formation, recognition, and degradation are drawn primarily from large gene families which have multiple representatives encoded by most bacterial genomes. Degradation of c-di-GMP is mediated by two families of specific PDEs called EAL and HDGYP proteins based on a stereotyped amino acid sequence and these proteins once again have a broad and frequently redundant phylogenetic distribution. motif present in their active sites. The chapter focuses on the EAL proteins that are most abundant and structurally best characterized. The exact separation between the c-di-GMP switch and the N-terminal β-strand of the PilZ domain varies in different family members, as does the conformation of this β-strand in some family members, which enables the switch to effect distinct changes in interdomain interactions in different PilZ domain-containing receptors. Ironically, neither the PilZ protein nor the XC1028 protein binds c-di-GMP in biochemical assays, and the structure of XC1028 does not contain either c-di-GMP binding motif described. Nuclear magnetic resonance (NMR) spectroscopy was used to determine the structure of PA4608 from Pseudomonas aeruginosa, which provided the first view of PilZ domain architecture. c-di-GMP is an exquisite multivalent molecule that can immobilize disordered protein segments or change the relative orientation of protein domains." @default.
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• W1433012466 date "2014-04-30" @default.
• W1433012466 modified "2023-09-26" @default.
• W1433012466 title "Making, Breaking, and Sensing of Cyclic Di-GMP: Structural, Thermodynamic, and Evolutionary Principles" @default.
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• W1433012466 doi "https://doi.org/10.1128/9781555816667.ch7" @default.
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