1xu3

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[[Image:1xu3.gif|left|200px]]
 
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==Soluble methane monooxygenase hydroxylase-soaked with bromophenol==
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The line below this paragraph, containing "STRUCTURE_1xu3", creates the "Structure Box" on the page.
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<StructureSection load='1xu3' size='340' side='right'caption='[[1xu3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1xu3]] 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=1XU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XU3 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BML:4-BROMOPHENOL'>BML</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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{{STRUCTURE_1xu3| PDB=1xu3 | SCENE= }}
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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=1xu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu3 OCA], [https://pdbe.org/1xu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1xu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xu3 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/xu/1xu3_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=1xu3 ConSurf].
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<div style="clear:both"></div>
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'''Soluble methane monooxygenase hydroxylase-soaked with bromophenol'''
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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 soluble methane monooxygenase hydroxylase (MMOH) alpha-subunit contains a series of cavities that delineate the route of substrate entrance to and product egress from the buried carboxylate-bridged diiron center. The presence of discrete cavities is a major structural difference between MMOH, which can hydroxylate methane, and toluene/o-xylene monooxygenase hydroxylase (ToMOH), which cannot. To understand better the functions of the cavities and to investigate how an enzyme designed for methane hydroxylation can also accommodate larger substrates such as octane, methylcubane, and trans-1-methyl-2-phenylcyclopropane, MMOH crystals were soaked with an assortment of different alcohols and their X-ray structures were solved to 1.8-2.4 A resolution. The product analogues localize to cavities 1-3 and delineate a path of product exit and/or substrate entrance from the active site to the surface of the protein. The binding of the alcohols to a position bridging the two iron atoms in cavity 1 extends and validates previous crystallographic, spectroscopic, and computational work indicating this site to be where substrates are hydroxylated and products form. The presence of these alcohols induces perturbations in the amino acid side-chain gates linking pairs of cavities, allowing for the formation of a channel similar to one observed in ToMOH. Upon binding of 6-bromohexan-1-ol, the pi helix formed by residues 202-211 in helix E of the alpha-subunit is extended through residue 216, changing the orientations of several amino acid residues in the active site cavity. This remarkable secondary structure rearrangement in the four-helix bundle has several mechanistic implications for substrate accommodation and the function of the effector protein, MMOB.
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[[Category: Large Structures]]
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==About this Structure==
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1XU3 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=1XU3 OCA].
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==Reference==
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Product bound structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): protein motion in the alpha-subunit., Sazinsky MH, Lippard SJ, J Am Chem Soc. 2005 Apr 27;127(16):5814-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15839679 15839679]
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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: Sazinsky MH]]
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[[Category: Sazinsky, M H.]]
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[[Category: Cavity]]
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[[Category: Diiron]]
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[[Category: Four-helix bundle]]
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[[Category: Methane]]
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[[Category: Substrate binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:30:36 2008''
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Current revision

Soluble methane monooxygenase hydroxylase-soaked with bromophenol

PDB ID 1xu3

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