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Literature summary extracted from

  • Myung Choi, J.; Cao, T.P.; Wouk Kim, S.; Ho Lee, K.; Haeng Lee, S.
    MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements (2017), Proteins, 85, 1379-1386 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.2.7 gene mxaJ, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of MxaJ(residues 12-281) excluding the signal peptide as a selennomethionine-labeled, N-terminally His6-tagged protein in Escherichia coli strain BL21(DE3), but the His-tag is removed by an Escherichia coli protease during expression Methylophaga aminisulfidivorans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.2.7 purified recombinant MxaJ(residues 12-281), hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M sodium bromide, 20% w/v PEG 3350, and 10% w/v glycerol, at 20°C, X-ray diffraction structure determination and analysis at 1.92 A resolution, modeling Methylophaga aminisulfidivorans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.7 extracellular solute-binding protein MxaJ Methylophaga aminisulfidivorans
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.2.7 145000
-
 MDHI Methylophaga aminisulfidivorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.7 methanol + 2 cytochrome cL Methylophaga aminisulfidivorans
-
 formaldehyde + 2 reduced cytochrome cL
-
 ?
1.1.2.7 methanol + 2 cytochrome cL Methylophaga aminisulfidivorans MP
-
 formaldehyde + 2 reduced cytochrome cL
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.7 Methylophaga aminisulfidivorans A3FJ48 AND A3FJ51 AND A3FJ49 subunits alpha and beta, and extracellular solute-binding protein MxaJ
-
1.1.2.7 Methylophaga aminisulfidivorans MP A3FJ48 AND A3FJ51 AND A3FJ49 subunits alpha and beta, and extracellular solute-binding protein MxaJ
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.2.7 recombinant selennomethionine-labeled, detagged MxaJ(residues 12-281) without signal peptide from Escherichia coli strain BL21(DE3) by anion-exchange chromatography and gel filtration Methylophaga aminisulfidivorans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.7 methanol + 2 cytochrome cL
-
 Methylophaga aminisulfidivorans formaldehyde + 2 reduced cytochrome cL
-
 ?
1.1.2.7 methanol + 2 cytochrome cL
-
 Methylophaga aminisulfidivorans MP formaldehyde + 2 reduced cytochrome cL
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.2.7 More the MxaJ molecule consists of nine alpha-helices (alpha1-alpha9) and six beta-strands (beta1-beta6), which are partitioned to form two globular domains (domain-1 and 2). The two domains are connected by a long and rigid beta-strand (beta3) at the center, and each domain has a different arrangement of alpha/beta secondary structural element. Detailed MxaJ structure analysis, overview Methylophaga aminisulfidivorans
1.1.2.7 tetramer alpha2beta2 MDH (MDHI) Methylophaga aminisulfidivorans

Synonyms

EC Number Synonyms Comment Organism
1.1.2.7 MDH
-
 Methylophaga aminisulfidivorans
1.1.2.7 MxaJ
-
 Methylophaga aminisulfidivorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.7 cytochrome cL UniProt ID A3FJ50 Methylophaga aminisulfidivorans
1.1.2.7 additional information MxaJ, a chaperone-like protein facilitating the assembly of MDH, additional component MxaJ together with a MDHI can facilitate the methanol oxidation process Methylophaga aminisulfidivorans
1.1.2.7 pyrroloquinoline quinone PQQ Methylophaga aminisulfidivorans

General Information

EC Number General Information Comment Organism
1.1.2.7 physiological function methanotrophic bacteria, including Methylophaga aminisulfidivorans, utilize methane as a carbon source to produce energy and organic chemicals. An alpha2beta2 MDH (MDHI) catalyzes the conversion of methanol to formaldehyde by transferring two electrons from methanol to Cyt cL. The MDH enzyme complex directly interacts with Cyt cL. The electrostatic and hydrophobic interactions are critical for the complex formation between MDH and Cyt cL. Cyt cL reaches the pyrroloquinoline quinone (PQQ) site in alpha-subunit of MDHI to transfer the electrons. MxaJ has a protein-binding site Methylophaga aminisulfidivorans