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Literature summary for 3.1.4.52 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Bdellovibrio bacteriovorus Q6MM30
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Synonyms

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

General Information

General Information Comment Organism
additional information Bd1817 lacks the active-site tyrosine present in most HD-GYP family members Bdellovibrio bacteriovorus
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