Crystallization (Comment) | Organism |
---|---|
X-ray diffraction structure determination and analysis at 1.94 A resolution | Methylorubrum extorquens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Methylorubrum extorquens | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required for activity, one of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group | Methylorubrum extorquens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + ferricytochrome cL | Methylorubrum extorquens | - |
formaldehyde + ferrocytochrome cL | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylorubrum extorquens | P16027 and P14775 | P16027 (large subunit, alpha) and P14775 (small subunit, beta) | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + ferricytochrome cL | - |
Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? | |
additional information | active site structure with important disulfide bridge of Cys103-Cys104, overview | Methylorubrum extorquens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | alpha2beta2, the alpha-subunit has an 8fold radial symmetry, with its eight 3-sheets stabilized by a novel tryptophan docking motif. The PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond, subunit structures and interactions, overview | Methylorubrum extorquens |
Synonyms | Comment | Organism |
---|---|---|
quinoprotein methanol dehydrogenase | - |
Methylorubrum extorquens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group | Methylorubrum extorquens |