1mmo
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CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE
OverviewOverview
The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric, hydroxylase protein of methane monooxygenase from Methylococcus capsulatus, (Bath) reveals the geometry of the catalytic di-iron core. The two iron, atoms are bridged by exogenous hydroxide and acetate ligands and further, coordinated by four glutamate residues, two histidine residues and a water, molecule. The dinuclear iron centre lies in a hydrophobic active-site, cavity for binding methane. An extended canyon runs between alpha beta, pairs, which have many long alpha-helices, for possible docking of the, reductase and coupling proteins required for catalysis.
About this StructureAbout this Structure
1MMO is a Protein complex structure of sequences from Methylococcus capsulatus with FE and ACY as ligands. Active as Methane monooxygenase, with EC number 1.14.13.25 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane., Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P, Nature. 1993 Dec 9;366(6455):537-43. PMID:8255292
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