Literature summary for 1.1.2.7 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 .

Search for more literature for 1.1.2.7

Cloned(Commentary)

Cloned (Comment)	Organism
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)

Crystallization (Comment)	Organism
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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
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)

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

Subunits

Subunits	Comment	Organism
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
tetramer	alpha2beta2 MDH (MDHI)	Methylophaga aminisulfidivorans

Synonyms

Synonyms	Comment	Organism
MDH	-	Methylophaga aminisulfidivorans
MxaJ	-	Methylophaga aminisulfidivorans

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome cL	UniProt ID A3FJ50	Methylophaga aminisulfidivorans
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
pyrroloquinoline quinone	PQQ	Methylophaga aminisulfidivorans

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)