1mmo

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[[Image:1mmo.gif|left|200px]]<br /><applet load="1mmo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mmo.gif|left|200px]]
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caption="1mmo, resolution 2.2&Aring;" />
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'''CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE'''<br />
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{{Structure
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|PDB= 1mmo |SIZE=350|CAPTION= <scene name='initialview01'>1mmo</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1MMO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMO OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8255292 8255292]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8255292 8255292]
[[Category: Methane monooxygenase]]
[[Category: Methane monooxygenase]]
[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
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[[Category: oxidoreductase (monooxygenase)]]
[[Category: oxidoreductase (monooxygenase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:27 2008''

Revision as of 10:45, 20 March 2008


PDB ID 1mmo

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: and
Activity: Methane monooxygenase, with EC number 1.14.13.25
Coordinates: save as pdb, mmCIF, xml



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. 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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