Crystallization (Comment) | Organism |
---|---|
purified recombinant DraG in the holo and ADP-ribose bound forms and a reaction intermediate analogue, sitting drop vapor diffusion method, 0.0006 ml of of 10 mg/ml wild-type DraG is mixed with an equal volume of 15% PEG 3350, 0.3 M NH4Cl, and 0.1 M Tris, pH 7.0, several days, cryoprotection in 20% PEG 3350, 0.3 M NH4Cl, 0.1M Tris, pH 7.0, and 20% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling, overview | Rhodospirillum rubrum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | DraG reversibly associates with the cell membrane | Rhodospirillum rubrum | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | two manganese ions per enzyme molecule bound at the active site, structure of the dinuclear binding site, overview. DraG shows a preference for manganese over magnesium, although not requiring a redox active metal for the reaction | Rhodospirillum rubrum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP-ribosyl-[dinitrogen reductase] + H2O | Rhodospirillum rubrum | DraG removes ADP-ribose upon exposure of the bacteria to light or depletion of the nitrogen source added, regenerating the arginine guanidino group and activating the dinitrogenase reductase dimer | ADP-ribose + [dinitrogen reductase] | - |
? | |
additional information | Rhodospirillum rubrum | DraG is capable of auto ADP-ribosylation when in excess of ADP-ribose, this reaction can function as an autoregulatory mechanism in vivo | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodospirillum rubrum | P14300 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine | substrate binding structure and detailed catalytic mechanism for protein de-ADP-ribosylation involving ring opening of the substrate ribose, overview | Rhodospirillum rubrum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP-ribosyl-[dinitrogen reductase] + H2O | - |
Rhodospirillum rubrum | ADP-ribose + [dinitrogen reductase] | - |
? | |
ADP-ribosyl-[dinitrogen reductase] + H2O | DraG removes ADP-ribose upon exposure of the bacteria to light or depletion of the nitrogen source added, regenerating the arginine guanidino group and activating the dinitrogenase reductase dimer | Rhodospirillum rubrum | ADP-ribose + [dinitrogen reductase] | - |
? | |
additional information | DraG is capable of auto ADP-ribosylation when in excess of ADP-ribose, this reaction can function as an autoregulatory mechanism in vivo | Rhodospirillum rubrum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Rhodospirillum rubrum |
Synonyms | Comment | Organism |
---|---|---|
mono-ADP-ribosylhydrolase | - |
Rhodospirillum rubrum |
General Information | Comment | Organism |
---|---|---|
physiological function | DraG is a key player in the regulation of nitrogenase activity. The enzyme, catalyzing removal of the ADP-ribose moiety, is involved in the reversible ADP-ribosylation, a ubiquitous regulatory posttranslational modification involved in numerous key processes such as DNA repair, transcription, cell differentiation, apoptosis, and the pathogenic mechanism of certain bacterial toxins | Rhodospirillum rubrum |