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Literature summary extracted from

  • Lovering, A.L.; Capeness, M.J.; Lambert, C.; Hobley, L.; Sockett, R.E.
    The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases (2011), mBio, 2, e00163.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.52 sequence comparisons, comparative transcriptional profiling of Bd1817 expression Bdellovibrio bacteriovorus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.52 crystals are grown by hanging-drop method at 18°C using 0.001 ml of protein solution mixed with an equal volume of reservoir solution, varying conditions using 0.1 M bis-Tris, pH 5.5, 0.2-0.4 M ammonium acetate, 25% w/v PEG 3350, with or without 20% v/v DMSO or 2.1 M DL-malic acid, pH 7.0, X-ray diffraction structure determination and analysis at 2.5 A resolution Bdellovibrio bacteriovorus

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.52 Bdellovibrio bacteriovorus Q6MM30
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Synonyms

EC Number Synonyms Comment Organism
3.1.4.52 Bd1817
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Bdellovibrio bacteriovorus
3.1.4.52 cyclic-di-GMP phosphodiesterase
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Bdellovibrio bacteriovorus
3.1.4.52 EAL
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Bdellovibrio bacteriovorus
3.1.4.52 HD-GYP
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Bdellovibrio bacteriovorus

General Information

EC Number General Information Comment Organism
3.1.4.52 additional information Bd1817 lacks the active-site tyrosine present in most HD-GYP family members Bdellovibrio bacteriovorus
3.1.4.52 physiological function the fold and active site of the HD-GYP domain are different from those of EAL proteins, and restricted access to the active-site cleft is indicative of a different mode of activity regulation. The region encompassing the GYP motif has a novel conformation and is surface exposed and available for complexation with binding partners, including GGDEF proteins. Structure of the GYP motif and structure-function relationship. Mechanistic implications for HD-GYP family proteins Bdellovibrio bacteriovorus