1mty: Difference between revisions
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[[Category: methane monooxygenase]] | [[Category: methane monooxygenase]] | ||
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Revision as of 10:59, 30 October 2007
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METHANE MONOOXYGENASE HYDROXYLASE FROM METHYLOCOCCUS CAPSULATUS (BATH)
OverviewOverview
The crystal structure of the nonheme iron-containing hydroxylase component, of methane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus, (Bath) has been solved in two crystal forms, one of which was refined to, 1.7 A resolution. The enzyme is composed of two copies each of three, subunits (alpha 2 beta 2 gamma 2), and all three subunits are almost, completely alpha-helical, with the exception of two beta hairpin, structures in the alpha subunit. The active site of each alpha subunit, contains one dinuclear iron center, housed in a four-helix bundle. The two, iron atoms are octahedrally coordinated by 2 histidine and 4 glutamic acid, residues as well as by a bridging hydroxide ion, a terminal water, molecule, and at 4 degrees C, a bridging acetate ion, which is replaced at, ... [(full description)]
About this StructureAbout this Structure
1MTY is a [Protein complex] structure of sequences from [Methylococcus capsulatus] with FE as [ligand]. Active as [Methane monooxygenase], with EC number [1.14.13.25]. Structure known Active Site: FE1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions., Rosenzweig AC, Brandstetter H, Whittington DA, Nordlund P, Lippard SJ, Frederick CA, Proteins. 1997 Oct;29(2):141-52. PMID:9329079
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