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Literature summary for extracted from

  • Williams, P.A.; Coates, L.; Mohammed, F.; Gill, R.; Erskine, P.T.; Coker, A.; Wood, S.P.; Anthony, C.; Cooper, J.B.
    The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens (2005), Acta Crystallogr. Sect. D, D61, 75-79.
    View publication on PubMed

Crystallization (Commentary)

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
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/ Products (Substrates)

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 and Products (Substrate)

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
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