EC Number   |
Reference |
|---|
   2.7.7.65 | after activation by berillium trifluoride. Activation causes rearrangement of an adaptor domain which in turn promotes dimer formation. The substrate analogue GTPgammaS and two putative cations are bound to the active sites. Identification of a second cyclic diguanylate binding mode that crosslinks the diguanylate cyclase domains within a protein dimer and results in noncompetitive product inhibition |
682885 |
| 2.7.7.65 | BeF3-/Mg2+-modified PleD (100 microM) in presence of cyclic di-3,5-guanylate (0.2 mM) and substrate-analog GTPalphaS (1 mM), hanging-drop vapour-diffusion: equal volumes protein solution (10 mg/ml) and precipitant solution (0.1M HEPES pH 8, 0.73 M Na2SO4), crystals: needle shape, space group: P2(1)2(1)2(1), unit cell parameters: a: 128.9, b: 132.6, c: 88.4, resolved by molecular replacement using PDB: 1W25 as model, tightened dimer interface at the dyad symmetric stem between D1/D2 domains of the two monomers upon rotation of D2 relative to D1, restructured beta4alpha4 loop compared to nonactivated state, GTPalphaS bound to both diguanylate cyclase (GGDEF) domain active sites, 2fold symmetric crosslinking of GGDEF domains of the structural dimer in presence of cyclic di-3,5-guanylate, cyclic di-3,5-guanylate bound to allosteric (inhibitory) site similarly to nonactivated state |
682885 |
| 2.7.7.65 | GcbC bound to c-di-GMP, X-ray diffraction structure determination and analysis |
761379 |
| 2.7.7.65 | in complex with cyclic di-3',5'-guanylate (PDB: 3BRE), solved by molecular replacement using PDB: 1W25 as model, tetramer of two anti-parallel dimers with physically blocked active site, hanging-drop vapour-diffusion: equal volumes protein solution (5-30 mg/ml) and reservoir solution (0.1 M Tris-HCl pH 8, 2.9 M NaCl, 15% xylitol), crystal: space group: C2, unit cell parameter: a: 144.5, b: 72.8, c: 106.1, beta: 110.8, asymmetric unit: two molecules with active site facing each other and four molecules cyclic di-3',5'-guanylate bound to residues Arg242 and Arg198 and two Mg2+ ions, resemblance of GAF domain assembly |
694796 |
| 2.7.7.65 | in complex with product cyclic diguanylate. The guanine base is H-bonded to N335 and D344, whereas the ribosyl and alpha-phosphate moieties extend over the beta2-beta3-hairpin that carries the GGEEF signature motif. In the crystal, cyclic diguanylate molecules are crosslinking active sites of adjacent dimers. In solution, two diguanylate cyclase doamins of a dimer may align in a twofold symmetric way to catalyze synthesis of cyclic diguanylate |
682502 |
| 2.7.7.65 | isoform GcbC physically interacting with its target protein at a conserved interface, and this interface can be predictive of diguanylate cyclase-target protein interactions. Physical interaction is necessary for the enzyme to maximally signal its target |
738964 |
| 2.7.7.65 | purified Lcd1GAF domain in complex with cAMP, sitting drop method, mixing 0.0015 ml of 8 mg/ml protein with 4 mM of cAMP and 0.0015 ml of 0.2 M sodium citrate and 20% w/v PEG 3350, 2-4 weeks at 18°C, X-ray diffraction structure determination and analysis at 2.15 A resolution, modelling |
761695 |
| 2.7.7.65 | purified recombinant periplasmic portion (residues 46-491, which includes the tandem PBPb-I and PBPb-II domains) of C-terminally His6-tagged CdgH, X-ray diffraction structure determination and analysis at 2.6 A resolution |
762429 |
| 2.7.7.65 | purified recombinant truncated enzymes SadC323-487 and SadC300-487, X-ray diffraction structure determination and analysis at 1.8 A and 2.8 A resolution, respectively. The structure contains ine Mg2+, molecular replacement structure analysis |
760992 |
| 2.7.7.65 | structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF omain in apo and substrate-bound forms. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. Enzyme forms a constitutive dimer and in this form its enzymatic activity is regulated by oxygen binding. The middle domain of DosC connects the sensory and effector modules and is likely to be both essential for and directly involved in the intramolecular signal transduction in DosC |
737355 |
