EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.7.7 | expression of N-terminally GST-tagged (ChlN/ChlB)2 complex | Thermosynechococcus vestitus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.3.7.7 | native and SeMet-labeled catalytic (ChlN/ChlB)2 complex, hanging drop vapor diffusion, 17°C, mixing of 0.003 ml of 10 mg/ml protein in 100 mM HEPES-NaOH, pH 7.5, 150 mM NaCl, and 10 mM MgCl2, with 0.003 ml of reservoir solution consisting of 9.5% PEG 6000, 85 mM HEPES-NaOH, pH 7.1, 14.3% 2-methyl pentane-2,4-diol, and 15% glycerol as cryoprotectants or 10.5% PEG 6000, 85 mM HEPES-NaOH, pH7.5, 14.3% 2-methyl pentane-2,4-diol, and 15% glycerol as cryoprotectants for selenomethionine-labeled protein, 3-5 days,X-ray diffraction structure determination and analysis at 2.4-2.81 A resolution | Thermosynechococcus vestitus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.7.7 | C95A | inactive protein, probably due to destabilization of the [4Fe-4S] cluster environment | Thermosynechococcus vestitus |
1.3.7.7 | C95S | inactive protein, probably due to destabilization of the [4Fe-4S] cluster environment | Thermosynechococcus vestitus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.3.7.7 | Fe2+ | the enzyme contains intersubunit [4Fe-4S] cluster in the homodimer formed by two ChlL subunits. The [4Fe-4S] cluster coordinated by an aspartate oxygen alongside three cysteine ligands, structure, overview | Thermosynechococcus vestitus | |
1.3.7.7 | Mg2+ | - |
Thermosynechococcus vestitus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.7.7 | chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | Thermosynechococcus vestitus | - |
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.7.7 | Thermosynechococcus vestitus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.3.7.7 | recombinant N-terminally GST-tagged (ChlN/ChlB)2 complex by glutathione affinity chromatography, and gel filtration and ultrafiltration | Thermosynechococcus vestitus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.7.7 | chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | - |
Thermosynechococcus vestitus | protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+ | - |
? | |
1.3.7.7 | chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | ferredoxin provides a single electron to ChlL2, which in turn transfers an electron to (ChlN/ChlB)2. Hydrolysis of the two ATP molecules results in the dissociation of ChlL2 from reduced (ChlN/ChlB)2. Protochlorophyllide reduction is completed after two sequential catalytic redox cycles. Substrate recognition by (ChlN/ChlB)2 essentially involves all functional groups of the substrate, modeling of the substrate binding site of (ChlN/ChlB)2, overview. Electron transfer pathway via the various redox centers of DPOR to the substrate, overview | Thermosynechococcus vestitus | protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+ | - |
? | |
1.3.7.7 | additional information | the invitro assay is performed with purified recombinant GST-tagged (ChlN/ChlB)2 complex and a ChlL2 subunit purified from Prochlorococcus marinus | Thermosynechococcus vestitus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.3.7.7 | heterooctamer | (alpha2)2(betagamma)4, DPOR is composed of the subunits ChlL, ChlN, and ChlB. Homodimeric ChlL2 bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase transferring single electrons to the heterotetrameric (ChlN/ChlB)2 complex. The latter contains two intersubunit [4Fe-4S] clusters and two protochlorophyllide binding sites, respectively, structure analysis of the catalytic (ChlN/ChlB)2 complex, overview. Subunits ChlN and ChlB exhibit a related architecture of three subdomains each built around a central, parallel beta-sheet surrounded by alpha-helices. Two ChlL2 dimers simultaneously interact with the (ChlN/ChlB)2 tetramer, giving rise to a heterooctameric holoenzyme | Thermosynechococcus vestitus |
1.3.7.7 | More | model of the complete hetero-octameric DPOR and distance between cofactors, overview | Thermosynechococcus vestitus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.7.7 | dark operative protochlorophyllide oxidoreductase | - |
Thermosynechococcus vestitus |
1.3.7.7 | DPOR | - |
Thermosynechococcus vestitus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.7.7 | ATP | dependent on, the homodimeric ChlL2 bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase | Thermosynechococcus vestitus | |
1.3.7.7 | Ferredoxin | the enzyme contains intersubunit [4Fe-4S] cluster in the homodimer formed by two ChlL subunits. The [4Fe-4S] cluster coordinated by an aspartate oxygen alongside three cysteine ligands, structure, overview. Iron-sulfur cluster coordination in DPOR compared to nitrogenase, overview | Thermosynechococcus vestitus |