Crystallization (Comment) | Organism |
---|---|
purified holoenzyme, hanging-drop vapour-diffusion method, 3 ml of 15 mg/ml protein solution, 20 mM Tris buffer, pH 8.0, are placed on siliconized cover slips and mixed with an equal volume of well solution, the cover slip is sealed with high-vacuum grease over a 1 ml well containing 20% PEG 8000, pH 9.0, large crystals after two weeks, X-ray diffraction structure determination and analysis at 1.2 A resolution, modeling | Methylorubrum extorquens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Methylorubrum extorquens | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required, bound at the active site, interaction with the cofactor and the active site residues Arg331, Asp303, and Glu177, but not Asn261, structure overview | Methylorubrum extorquens | |
additional information | Mg2+ cannot substitute for Ca2+ | Methylorubrum extorquens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + ferricytochrome cL | Methylorubrum extorquens | the physiological electron acceptor is cytochrome cL. Cytochrome cL is subsequently oxidized by the small class I c-type cytochrome cH | formaldehyde + ferrocytochrome cL | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylorubrum extorquens | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ | active site structure with bound cofactor, the reduced pyrroloquinoline quinone (PQQ) transfers two electrons in single electron-transfer steps to cytochrome cL, creating a semiquinone form of the prosthetic group after the first electron transfer, electron transfer via enzyme residues Cys104, Asp105, and Asn52 | Methylorubrum extorquens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + ferricytochrome cL | terminal electron acceptor is cytochrome cL | Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? | |
methanol + ferricytochrome cL | the physiological electron acceptor is cytochrome cL. Cytochrome cL is subsequently oxidized by the small class I c-type cytochrome cH | Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the periplasmic protein contains both a PQQ-containing domain, folded into a beta-propeller fold, and a smaller cytochrome c domain, which is analogous to a typical class I c-type cytochrome, these two domains are connected via a proline-rich linker region, which lacks any secondary structure, structure model of the electron-transfer complex formed by MDH and cytochrome cL, overview | Methylorubrum extorquens |
tetramer | alpha2beta2 subunit conposition, structure model of an alphabeta unit from crystal structure determination, overview | Methylorubrum extorquens |
Synonyms | Comment | Organism |
---|---|---|
MDH | - |
Methylorubrum extorquens |
methanol dehydrogenase | - |
Methylorubrum extorquens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview | Methylorubrum extorquens |