The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A

Ghosh, M.; Anthony, C.; Harlos, K.; Goodwin, M.G.; Blake, C.; Structure 3, 177-187 (1995)

show all sequences of 1.1.2.7

Data extracted from this reference:

Crystallization (Commentary)
Crystallization Organism
X-ray diffraction structure determination and analysis at 1.94 A resolution Methylobacterium extorquens NCIMB 9133
X-ray diffraction structure determination and analysis at 1.94 A resolution Methylobacterium extorquens
Localization
Localization Commentary Organism GeneOntology No. Textmining
periplasm
-
Methylobacterium extorquens
-
-
periplasm
-
Methylobacterium extorquens NCIMB 9133
-
-
Metals/Ions
Metals/Ions Commentary Organism Structure
Ca2+ required for activity, one of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group Methylobacterium extorquens
Natural Substrates/ Products (Substrates)
Natural Substrates Organism Commentary (Nat. Sub.) Natural Products Commentary (Nat. Pro.) Organism (Nat. Pro.) Reversibility
methanol + ferricytochrome cL Methylobacterium extorquens
-
formaldehyde + ferrocytochrome cL
-
-
?
Organism
Organism Primary Accession No. (UniProt) Commentary Textmining
Methylobacterium extorquens P16027 and P14775 P16027 (large subunit, alpha) and P14775 (small subunit, beta)
-
Substrates and Products (Substrate)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
methanol + ferricytochrome cL
-
690095 Methylobacterium extorquens formaldehyde + ferrocytochrome cL
-
-
-
?
More active site structure with important disulfide bridge of Cys103-Cys104, overview 690095 Methylobacterium extorquens ?
-
-
-
-
More active site structure with important disulfide bridge of Cys103-Cys104, overview 690095 Methylobacterium extorquens NCIMB 9133 ?
-
-
-
-
Subunits
Subunits Commentary Organism
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 Methylobacterium extorquens
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 Methylobacterium extorquens NCIMB 9133
Cofactor
Cofactor Commentary Organism Structure
pyrroloquinoline quinone dependent on, prosthetic group, 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. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group Methylobacterium extorquens
Cofactor (protein specific)
Cofactor Commentary Organism Structure
pyrroloquinoline quinone dependent on, prosthetic group, 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. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group Methylobacterium extorquens
Crystallization (Commentary) (protein specific)
Crystallization Organism
X-ray diffraction structure determination and analysis at 1.94 A resolution Methylobacterium extorquens
X-ray diffraction structure determination and analysis at 1.94 A resolution Methylobacterium extorquens NCIMB 9133
Localization (protein specific)
Localization Commentary Organism GeneOntology No. Textmining
periplasm
-
Methylobacterium extorquens
-
-
periplasm
-
Methylobacterium extorquens NCIMB 9133
-
-
Metals/Ions (protein specific)
Metals/Ions Commentary Organism Structure
Ca2+ required for activity, one of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group Methylobacterium extorquens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates Organism Commentary (Nat. Sub.) Natural Products Commentary (Nat. Pro.) Organism (Nat. Pro.) Reversibility
methanol + ferricytochrome cL Methylobacterium extorquens
-
formaldehyde + ferrocytochrome cL
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
methanol + ferricytochrome cL
-
690095 Methylobacterium extorquens formaldehyde + ferrocytochrome cL
-
-
-
?
More active site structure with important disulfide bridge of Cys103-Cys104, overview 690095 Methylobacterium extorquens ?
-
-
-
-
More active site structure with important disulfide bridge of Cys103-Cys104, overview 690095 Methylobacterium extorquens NCIMB 9133 ?
-
-
-
-
Subunits (protein specific)
Subunits Commentary Organism
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 Methylobacterium extorquens
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 Methylobacterium extorquens NCIMB 9133


See also following references to EC number 1.1.2.7 (sorted by year of publication):
No.1st authorPub
Med
titleorganimsjournalvolumepagesyearActivating CompoundApplicationCloned(Commentary)Crystallization (Commentary)EngineeringGeneral StabilityInhibitorsKM Value [mM]LocalizationMetals/IonsMolecular Weight [Da]Natural Substrates/ Products (Substrates)Organic Solvent StabilityOrganismOxidation StabilityPosttranslational ModificationPurification (Commentary)ReactionRenatured (Commentary)Source TissueSpecific Activity [micromol/min/mg]Storage StabilitySubstrates and Products (Substrate)SubunitsTemperature Optimum [°C]Temperature Range [°C]Temperature Stability [°C]Turnover Number [1/s]pH OptimumpH RangepH StabilityCofactorKi Value [mM]pI ValueIC50 ValueActivating Compound (protein specific)Application (protein specific)Cloned(Commentary) (protein specific)Cofactor (protein specific)Crystallization (Commentary) (protein specific)Engineering (protein specific)General Stability (protein specific)IC50 Value (protein specific)Inhibitors (protein specific)Ki Value [mM] (protein specific)KM Value [mM] (protein specific)Localization (protein specific)Metals/Ions (protein specific)Molecular Weight [Da] (protein specific)Natural Substrates/ Products (Substrates) (protein specific)Organic Solvent Stability (protein specific)Oxidation Stability (protein specific)Posttranslational Modification (protein specific)Purification (Commentary) (protein specific)Renatured (Commentary) (protein specific)Source Tissue (protein specific)Specific Activity [micromol/min/mg] (protein specific)Storage Stability (protein specific)Substrates and Products (Substrate) (protein specific)Subunits (protein specific)Temperature Optimum [°C] (protein specific)Temperature Range [°C] (protein specific)Temperature Stability [°C] (protein specific)Turnover Number [1/s] (protein specific)pH Optimum (protein specific)pH Range (protein specific)pH Stability (protein specific)pI Value (protein specific)ExpressionGeneral InformationGeneral Information (protein specific)Expression (protein specific)KCat/KM [mM/s]KCat/KM [mM/s] (protein specific)
712855IdupulapatiQuantum chemical modeling of m ...Methylobacterium extorquensJ. Phys. Chem. A1141887-18962010---3-----1---1-------------------------3-------1--------------------------
687417KalyuzhnayaCharacterization of a novel me ...Methylibium petroleiphilum, Methyloversatilis universalisJ. Bacteriol.1903817-382320082-2----82--2-7--------1022---2--4---2-24------82--2--------1022---2---------
673047LeopoldiniThe preferred reaction path fo ...Methylophilus methylotrophusChem. Eur. J.132109-21172007-------111---1---3-----1-------1------1------111-----------1--------------
676902ZhangMechanism of methanol oxidatio ...Methylophilus methylotrophusProc. Natl. Acad. Sci. USA104745-7492007---------1---2---1-------------1------1--------1--------------------------
667721NojiriCrystal structures of cytochro ...Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151Biochemistry453481-34922006---2---11--22-5--2---3-332--1211-4------42-----11--22---2--3-322--1211--------
670785LiuA rapid method for the purific ...Methylobacterium extorquensProtein Expr. Purif.46316-3202006-----2---2---1--2---24-2----1--2-1----2--2-----2-----2--24-2----1--1------
688333WilliamsThe 1.6A X-ray structure of th ...Methylobacterium extorquensJ. Mol. Biol.357151-1622006---------1-1-4--------2--------3------3--------1-1--------2---------------
671068WilliamsThe atomic resolution structur ...Methylobacterium extorquensActa Crystallogr. Sect. DD6175-792005---3----32-1-1---1----22-------1------13------32-1--------22--------------
673048Nojiri-Preparation and characterizati ...Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151Chem. Lett.341036-10372005--2-2----2---2--22--5--2-------2-----22-2------2-----2--5--2--------------
684666AnthonyThe quinoprotein dehydrogenase ...Methylobacterium extorquens, Methylophilus sp.Arch. Biochem. Biophys.4282-92004---4---444-3-4---4----63----1--7------74-----444-3--------63----1---------
685313AnthonyThe structure and mechanism of ...Methylobacterium extorquens, Methylophilus sp.Biochim. Biophys. Acta164718-2320034--42---44-3-2--------6--------3---4--342-----44-3--------6---------------
687993JongejanDirect hydride transfer in the ...Methylobacterium extorquens, Methylophilus methylotrophusJ. Comput. Chem.221732-17492001---------2---2---2----3--------2------2--------2----------3---------------
689818ZhengCatalytic mechanism of quinopr ...Methylophilus methylotrophusProc. Natl. Acad. Sci. USA98432-4342001---------1---3-----------------1------1--------1--------------------------
687432GrossePurification and properties of ...Methylosinus sp., Methylosinus sp. WI 14J. Basic Microbiol.38189-19619984-----5142-21-2--2---241222-2-1--2---4--2----5-142-21---2--241222-2-1---------
689815ZhengConformation of coenzyme pyrro ...Methylophilus methylotrophusProc. Natl. Acad. Sci. USA9411881-118861997---------1---2-----------------1------1--------1--------------------------
684950GoodwinReconstitution of the quinopro ...Methylobacterium extorquensBiochem. J.319839-8421996----2---33-1-3----2---1-2---11-3------3-2-----33-1----2---1-2---11--------
684948AvezouxThe role of the novel disulphi ...Methylobacterium extorquensBiochem. J.307735-7411995----2----3---4--------1-2---1--4------4-2------3----------1-2---1---------
690095GhoshThe refined structure of the q ...Methylobacterium extorquensStructure3177-1871995---2----21-1-4--------32-------1------12------21-1--------32--------------
690794CozierThe structure of the quinoprot ...Methylobacterium extorquensBiochem. J.308375-3791995---2----33-2-1--------22-------4------42------33-2--------22--------------
689139BlakeThe active site of methanol de ...Methylobacterium extorquensNat. Struct. Biol.1102-1051994---------2-2-4--------41-------1------1--------2-2--------41--------------
685050WhiteThe active site structure of t ...Methylophilus sp., Methylophilus sp. W3A1Biochemistry3212955-129581993---------2---3---------2-------2------2--------2-----------2--------------
684947RichardsonCharacterization of mutant for ...Methylobacterium extorquens, Methylobacterium extorquens NCIMB 9133Biochem. J.287709-7151992----2-2--1---7----2----22---1--1------1-2--2---1------2----22---1---------
687486XiaThe three-dimensional structur ...Methylophilus methylotrophusJ. Biol. Chem.26722289-222971992---1----1-1--1---------1-------1------11------1-1----------1--------------