1mmo
From Proteopedia
(New page: 200px<br /><applet load="1mmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mmo, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1mmo.gif|left|200px]]<br /><applet load="1mmo" size=" | + | [[Image:1mmo.gif|left|200px]]<br /><applet load="1mmo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mmo, resolution 2.2Å" /> | caption="1mmo, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE'''<br /> | '''CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric | + | The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric hydroxylase protein of methane monooxygenase from Methylococcus capsulatus (Bath) reveals the geometry of the catalytic di-iron core. The two iron atoms are bridged by exogenous hydroxide and acetate ligands and further coordinated by four glutamate residues, two histidine residues and a water molecule. The dinuclear iron centre lies in a hydrophobic active-site cavity for binding methane. An extended canyon runs between alpha beta pairs, which have many long alpha-helices, for possible docking of the reductase and coupling proteins required for catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1MMO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] with FE and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1MMO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1MMO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Frederick, C | + | [[Category: Frederick, C A.]] |
| - | [[Category: Lippard, S | + | [[Category: Lippard, S J.]] |
[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
| - | [[Category: Rosenzweig, A | + | [[Category: Rosenzweig, A C.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: FE]] | [[Category: FE]] | ||
[[Category: oxidoreductase (monooxygenase)]] | [[Category: oxidoreductase (monooxygenase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:44 2008'' |
Revision as of 11:56, 21 February 2008
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CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE
Overview
The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric hydroxylase protein of methane monooxygenase from Methylococcus capsulatus (Bath) reveals the geometry of the catalytic di-iron core. The two iron atoms are bridged by exogenous hydroxide and acetate ligands and further coordinated by four glutamate residues, two histidine residues and a water molecule. The dinuclear iron centre lies in a hydrophobic active-site cavity for binding methane. An extended canyon runs between alpha beta pairs, which have many long alpha-helices, for possible docking of the reductase and coupling proteins required for catalysis.
About this Structure
1MMO is a Protein complex structure of sequences from Methylococcus capsulatus with and as ligands. Active as Methane monooxygenase, with EC number 1.14.13.25 Full crystallographic information is available from OCA.
Reference
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane., Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P, Nature. 1993 Dec 9;366(6455):537-43. PMID:8255292
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