1tvc
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1tvc.gif|left|200px]] | [[Image:1tvc.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1tvc", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1tvc| PDB=1tvc | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)''' | '''FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)''' | ||
| Line 31: | Line 28: | ||
[[Category: Mueller, J.]] | [[Category: Mueller, J.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
| - | [[Category: | + | [[Category: Fad-binding]] |
| - | [[Category: | + | [[Category: Nadh-binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:24:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:24, 3 May 2008
FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)
Overview
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
1TVC is a Single protein structure of sequence from Methylococcus capsulatus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 10:24:46 2008
