EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.4.52 | sequence comparisons, comparative transcriptional profiling of Bd1817 expression | Bdellovibrio bacteriovorus |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.52 | Bdellovibrio bacteriovorus | Q6MM30 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.4.52 | Bd1817 | - |
Bdellovibrio bacteriovorus |
3.1.4.52 | cyclic-di-GMP phosphodiesterase | - |
Bdellovibrio bacteriovorus |
3.1.4.52 | EAL | - |
Bdellovibrio bacteriovorus |
3.1.4.52 | HD-GYP | - |
Bdellovibrio bacteriovorus |
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 |