1tvc: Difference between revisions
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New page: left|200px<br /><applet load="1tvc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tvc" /> '''FAD and NADH binding domain of methane monoo... |
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[[Image:1tvc.gif|left|200px]]<br /><applet load="1tvc" size=" | [[Image:1tvc.gif|left|200px]]<br /><applet load="1tvc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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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.]] | ||
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[[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'' | ||
