1jq4
From Proteopedia
(New page: 200px<br /><applet load="1jq4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jq4" /> '''[2Fe-2S] Domain of Methane Monooxygenase Red...) |
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'''[2Fe-2S] Domain of Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)'''<br /> | '''[2Fe-2S] Domain of Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The soluble methane monooxygenase (sMMO) from Methylococcus capsulatus | + | 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we report the solution structure of the reduced form of the 98-amino acid Fd domain (Blazyk, J. L., and Lippard, S. J. Unpublished results) determined by nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations.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== | ==About this Structure== | ||
| - | 1JQ4 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 FES 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:// | + | 1JQ4 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=FES:'>FES</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=1JQ4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lippard, S | + | [[Category: Lippard, S J.]] |
| - | [[Category: Lugovskoy, A | + | [[Category: Lugovskoy, A A.]] |
[[Category: Mueller, J.]] | [[Category: Mueller, J.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
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[[Category: [2fe-2s] ferredoxin]] | [[Category: [2fe-2s] ferredoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:32 2008'' |
Revision as of 11:25, 21 February 2008
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[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 with as ligand. Active as Methane monooxygenase, with EC number 1.14.13.25 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[[Category: [2fe-2s] ferredoxin]]
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