1tvc: Difference between revisions
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'''FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)'''<br /> | '''FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)'''<br /> | ||
==Overview== | ==Overview== | ||
Soluble methane monooxygenase (sMMO) catalyzes the hydroxylation of | Soluble methane monooxygenase (sMMO) catalyzes the hydroxylation of methane by dioxygen to methanol, the first step in carbon assimilation by methanotrophs. This multicomponent system transfers electrons from NADH through a reductase component to the non-heme diiron center in the hydroxylase where O(2) is activated. The reductase component comprises three distinct domains, a [2Fe-2S] ferredoxin domain along with FAD- and NADH-binding domains. We report the solution structure of the reduced 27.6 kDa FAD- and NADH-binding domains (MMOR-FAD) of the reductase from Methylococcus capsulatus (Bath). The FAD-binding domain consists of a six-stranded antiparallel beta-barrel and one alpha-helix, with the first 10 N-terminal residues unstructured. In the interface between the two domains, the FAD cofactor is tightly bound in an unprecedented extended conformation. The NADH-binding domain consists of a five-stranded parallel beta-sheet with four alpha-helices packing closely around this sheet. MMOR-FAD is structurally homologous to other FAD-containing oxidoreductases, and we expect similar structures for the FAD/NADH-binding domains of reductases that occur in other multicomponent monooxygenases. | ||
==About this Structure== | ==About this Structure== | ||
1TVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] with FDA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] Full crystallographic information is available from [http:// | 1TVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] with <scene name='pdbligand=FDA:'>FDA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chatwood, L | [[Category: Chatwood, L L.]] | ||
[[Category: Gross, J | [[Category: Gross, J D.]] | ||
[[Category: Lippard, S | [[Category: Lippard, S J.]] | ||
[[Category: Mueller, J.]] | [[Category: Mueller, J.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
| Line 22: | Line 22: | ||
[[Category: fad-binding; nadh-binding]] | [[Category: fad-binding; nadh-binding]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:43 2008'' | ||
Revision as of 16:17, 21 February 2008
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FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)
OverviewOverview
Soluble methane monooxygenase (sMMO) catalyzes the hydroxylation of methane by dioxygen to methanol, the first step in carbon assimilation by methanotrophs. This multicomponent system transfers electrons from NADH through a reductase component to the non-heme diiron center in the hydroxylase where O(2) is activated. The reductase component comprises three distinct domains, a [2Fe-2S] ferredoxin domain along with FAD- and NADH-binding domains. We report the solution structure of the reduced 27.6 kDa FAD- and NADH-binding domains (MMOR-FAD) of the reductase from Methylococcus capsulatus (Bath). The FAD-binding domain consists of a six-stranded antiparallel beta-barrel and one alpha-helix, with the first 10 N-terminal residues unstructured. In the interface between the two domains, the FAD cofactor is tightly bound in an unprecedented extended conformation. The NADH-binding domain consists of a five-stranded parallel beta-sheet with four alpha-helices packing closely around this sheet. MMOR-FAD is structurally homologous to other FAD-containing oxidoreductases, and we expect similar structures for the FAD/NADH-binding domains of reductases that occur in other multicomponent monooxygenases.
About this StructureAbout this Structure
1TVC is a Single protein structure of sequence from Methylococcus capsulatus with as ligand. Active as Methane monooxygenase, with EC number 1.14.13.25 Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)., Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ, Biochemistry. 2004 Sep 28;43(38):11983-91. PMID:15379538
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