1.1.2.7 ? x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE -, 670785 1.1.2.7 dimer 2 * 70000, SDS-PAGE -, 687432 1.1.2.7 heterotetramer alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits -, 723854, 724176 1.1.2.7 monomer 1 * 18000, cytochrome cL, SDS-PAGE -, 763357 1.1.2.7 monomer in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein -, 687417 1.1.2.7 additional information in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methylibium petroleiphilum strain PM1 is a monosubunit protein 687417 1.1.2.7 additional information the alpha-subunit is known to function as the active site for the oxidoreduction reaction, which includes the PQQ group as a redox cofactor and a calcium ion coordinated to vicinal charged and hydrophobic amino-acid residues -, 723854 1.1.2.7 additional information the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5 -, 724402 1.1.2.7 additional information the large alpha-subunit has a propeller fold making up a superbarrel of eight radially arranged beta-sheets, i.e. the propeller blades, containing the tryptophan-docking motifs that link together the eight beta-sheets, and the presence in the active site of a unique eight-membered disulfide ring structure formed from adjacent cysteine residues 103 and 104, joined by an atypical non-planar peptide bond 684666 1.1.2.7 additional information 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 -, 763672 1.1.2.7 additional information the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex -, 725300 1.1.2.7 additional information the overall interaction between beta-subunits and alpha-subunits of Ma-MDH is stronger than that of terrestrial homologues, providing the structural integrity to Ma-MDH in aquatic environments -, 763357 1.1.2.7 additional information 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 671068 1.1.2.7 additional information three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview -, 724176 1.1.2.7 pentamer 2 * 65980, subunit alpha, + 2 * 7580, subunit beta, + 1 * 27860, MxaJ protein, type II MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer, and contains an additional MxaJ protein -, 725300 1.1.2.7 tetramer 2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination -, 673047 1.1.2.7 tetramer 2 * 65000 + 2 * 9000 -, 667721 1.1.2.7 tetramer 2 * 65000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE -, 673048 1.1.2.7 tetramer 2 * 65980, subunit alpha, + 2 * 7580, subunit beta, type I MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer -, 725300 1.1.2.7 tetramer 2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination 684666 1.1.2.7 tetramer 4 * 66000, alpha2beta2, crystal structure 690794 1.1.2.7 tetramer alpha2beta2 -, 687486 1.1.2.7 tetramer alpha2beta2 MDH (MDHI) -, 763672 1.1.2.7 tetramer alpha2beta2 structure, subunit organization and structure, docking model, overview -, 667721 1.1.2.7 tetramer alpha2beta2 subunit conposition, structure model of an alphabeta unit from crystal structure determination, overview 671068 1.1.2.7 tetramer alpha2beta2, comparison of wild-type and mutant enzyme structures, overview -, 684947 1.1.2.7 tetramer alpha2beta2, the alpha-subunit has an 8fold radial symmetry, with its eight 3-sheets stabilized by a novel tryptophan docking motif. The PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond, subunit structures and interactions, overview 690095 1.1.2.7 tetramer alpha2beta2, three-dimensional structure, modelling, overview 689139 1.1.2.7 tetramer heterotetramer, structure analysis and modelling, overview -, 685050