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1fz3

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[[Image:1fz3.gif|left|200px]]
 
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{{Structure
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==METHANE MONOOXYGENASE HYDROXYLASE, FORM III SOAK AT PH 6.2 (0.1 M PIPES)==
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|PDB= 1fz3 |SIZE=350|CAPTION= <scene name='initialview01'>1fz3</scene>, resolution 2.03&Aring;
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<StructureSection load='1fz3' size='340' side='right'caption='[[1fz3]], [[Resolution|resolution]] 2.03&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>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
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<table><tr><td colspan='2'>[[1fz3]] 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=1FZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FZ3 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]] 2.03&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=1fz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fz3 OCA], [https://pdbe.org/1fz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fz3 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/fz/1fz3_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=1fz3 ConSurf].
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<div style="clear:both"></div>
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'''METHANE MONOOXYGENASE HYDROXYLASE, FORM III SOAK AT PH 6.2 (0.1 M PIPES)'''
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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 oxidation of methane to methanol is performed at carboxylate-bridged dinuclear iron centers in the soluble methane monooxygenase hydroxylase (MMOH). Previous structural studies of MMOH, and the related R2 subunit of ribonucleotide reductase, have demonstrated the occurrence of carboxylate shifts involving glutamate residues that ligate the catalytic iron atoms. These shifts are thought to have important mechanistic implications. Recent kinetic and theoretical studies have also emphasized the importance of hydrogen bonding and pH effects at the active site. We report here crystal structures of MMOH from Methylococcus capsulatus (Bath) in the diiron(II), diiron(III), and mixed-valent Fe(II)Fe(III) oxidation states, and at pH values of 6.2, 7.0, and 8.5. These structures were investigated in an effort to delineate the range of possible motions at the MMOH active site and to identify hydrogen-bonding interactions that may be important in understanding catalysis by the enzyme. Our results present the first view of the diiron center in the mixed-valent state, and they indicate an increased lability for ferrous ions in the enzyme. Alternate conformations of Asn214 near the active site according to redox state and a distortion in one of the alpha-helices adjacent to the metal center in the diiron(II) state have also been identified. These changes alter the surface of the protein in the vicinity of the catalytic core and may have implications for small-molecule accessibility to the active site and for protein component interactions in the methane monooxygenase system. Collectively, these results help to explain previous spectroscopic observations and provide new insight into catalysis by the enzyme.
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[[Category: Large Structures]]
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==About this Structure==
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1FZ3 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=1FZ3 OCA].
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==Reference==
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Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site., Whittington DA, Lippard SJ, J Am Chem Soc. 2001 Feb 7;123(5):827-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11456616 11456616]
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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: Lippard SJ]]
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[[Category: Lippard, S J.]]
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[[Category: Whittington DA]]
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[[Category: Whittington, D A.]]
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[[Category: CA]]
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[[Category: FE]]
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[[Category: FMT]]
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[[Category: dinuclear iron center]]
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[[Category: monooxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:53 2008''
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Current revision

METHANE MONOOXYGENASE HYDROXYLASE, FORM III SOAK AT PH 6.2 (0.1 M PIPES)

PDB ID 1fz3

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