1jq4
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1jq4.gif|left|200px]] | [[Image:1jq4.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1jq4", 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_1jq4| PDB=1jq4 | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''[2Fe-2S] Domain of Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)''' | '''[2Fe-2S] Domain of Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)''' | ||
| Line 30: | Line 27: | ||
[[Category: Mueller, J.]] | [[Category: Mueller, J.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:36:24 2008'' | |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:36, 2 May 2008
[2Fe-2S] Domain of Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)
Overview
The soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a multicomponent enzyme system required for the conversion of methane to methanol. It comprises a hydroxylase, a regulatory protein, and a reductase. The reductase contains two domains: an NADH-binding and FAD-containing flavin domain and a ferredoxin (Fd) domain carrying a [2Fe-2S] cofactor. Here, we report the solution structure of the reduced form of the 98-amino acid Fd domain (Blazyk, J. L., and Lippard, S. J. Unpublished results) determined by nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations. The structure consists of six beta strands arranged into two beta sheets as well as three alpha helices. Two of these helices form a helix-proline-helix motif, unprecedented among [2Fe-2S] proteins. The [2Fe-2S] cluster is coordinated by the sulfur atoms of cysteine residues 42, 47, 50, and 82. The 10.9 kDa ferredoxin domain of the reductase protein transfers electrons to carboxylate-bridged diiron centers in the 251 kDa hydroxylase component of sMMO. The binding of the Fd domain with the hydroxylase was investigated by NMR spectroscopy. The hydroxylase binding surface on the ferredoxin protein has a polar center surrounded by patches of hydrophobic residues. This arrangement of amino acids differs from that by which previously studied [2Fe-2S] proteins interact with their electron-transfer partners. The critical residues on the Fd domain involved in this binding interaction map well onto the universally conserved residues of sMMO enzymes from different species. We propose that the [2Fe-2S] domains in these other sMMO systems have a fold very similar to the one found here for M. capsulatus (Bath) MMOR-Fd.
About this Structure
1JQ4 is a Single protein structure of sequence from Methylococcus capsulatus. Full crystallographic information is available from OCA.
Reference
NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase., Muller J, Lugovskoy AA, Wagner G, Lippard SJ, Biochemistry. 2002 Jan 8;41(1):42-51. PMID:11772001 Page seeded by OCA on Fri May 2 21:36:24 2008
