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InterPro: IPR003420 Methanol dehydrogenase, beta subunit

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30 proteins

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Accession

IPR003420 Meth_DH_bsu

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:4.10.160.10	Meth_DH_beta	28
Pfam	PF02315	MDH	30
PIRSF	PIRSF029163	Meth_DH_beta	25
SuperFamily	SSF48666	Meth_DH_beta	29
Signatures in BioMart

GO Term annotation Help

Process

GO:0015946 methanol oxidation
GO:0055114 oxidation reduction

Function

GO:0004022 alcohol dehydrogenase (NAD) activity

InterPro annotation

Entry Details in BioMart

Abstract

Methanol dehydrogenase (MDH) (EC:1.1.99.8), found in Gram-negative bacteria, is a pyrroloquinoline quinone (PQQ)-containing enzyme which oxidises methanol to formaldehyde. It is located in the periplasmic space and passes electrons derived from the oxidation of methanol to the soluble cytochrome cL [1]. The enzyme is a tetramer composed of two large alpha subunits and two smaller beta subunits. The alpha subunit binds the PQQ cofactor and contains the active site, while the function of the beta subunit is currently unknown [2]. The alpha subunit forms an eight-bladed propeller structure, with several novel tryptophan-docking motifs linking the individual blades together.

This entry represents the beta subunit of methanol dehydrogenase.

Structural links Help

PDB - click here

SCOP: a.137.2.1

CATH: 4.10.160.10

Database links Help

Enzyme: EC:1.1.99.8

PANDIT: PF02315

Blocks: IPB003420

Taxonomic coverage Help

Example proteins Help

P14775 Methanol dehydrogenase subunit 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003420	Methanol dehydrogenase, beta subunit
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Anthony C. The quinoprotein dehydrogenases for methanol and glucose. Arch. Biochem. Biophys. 428 2-9 2004 [PubMed: 15234264] http://dx.doi.org/10.1016/j.abb.2004.03.038
2.	Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C. Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L). Biochemistry 40 9799-809 2001 [PubMed: 11502173] http://dx.doi.org/10.1021/bi002932l

Additional Reading Open in usermanual
	Nojiri M, Hira D, Yamaguchi K, Okajima T, Tanizawa K, Suzuki S. Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins. Biochemistry 45 2006 3481-92 [PubMed: 16533029] http://dx.doi.org/10.1021/bi051877j
	Williams PA, Coates L, Mohammed F, Gill R, Erskine PT, Coker A, Wood SP, Anthony C, Cooper JB. The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens. Acta Crystallogr. D Biol. Crystallogr. 61 2005 75-9 [PubMed: 15608378] http://dx.doi.org/10.1107/S0907444904026964
	Xia ZX, Dai WW, He YN, White SA, Mathews FS, Davidson VL. X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i. J. Biol. Inorg. Chem. 8 2003 843-54 [PubMed: 14505072] http://dx.doi.org/10.1007/s00775-003-0485-0
	Zheng YJ, Xia Zx , Chen Zw , Mathews FS, Bruice TC. Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation. Proc. Natl. Acad. Sci. U.S.A. 98 2001 432-4 [PubMed: 11149955] http://dx.doi.org/10.1073/pnas.021547498
	Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C. The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A. Structure 3 1995 177-87 [PubMed: 7735834] http://dx.doi.org/10.1016/S0969-2126(01)00148-4

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