1mmo

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[[Image:1mmo.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE==
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|PDB= 1mmo |SIZE=350|CAPTION= <scene name='initialview01'>1mmo</scene>, resolution 2.2&Aring;
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<StructureSection load='1mmo' size='340' side='right'caption='[[1mmo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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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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<table><tr><td colspan='2'>[[1mmo]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMO FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmo OCA], [https://pdbe.org/1mmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmo RCSB], [https://www.ebi.ac.uk/pdbsum/1mmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MEMA_METCA MEMA_METCA] Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mmo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mmo ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE'''
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==See Also==
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*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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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].
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==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://www.ncbi.nlm.nih.gov/pubmed/8255292 8255292]
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[[Category: Methane monooxygenase]]
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[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
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[[Category: Protein complex]]
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[[Category: Frederick CA]]
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[[Category: Frederick, C A.]]
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[[Category: Lippard SJ]]
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[[Category: Lippard, S J.]]
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[[Category: Nordlund P]]
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[[Category: Nordlund, P.]]
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[[Category: Rosenzweig AC]]
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[[Category: Rosenzweig, A C.]]
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[[Category: ACY]]
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[[Category: FE]]
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[[Category: oxidoreductase (monooxygenase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:27 2008''
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Current revision

CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE

PDB ID 1mmo

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