View source for 1fzh


==METHANE MONOOXYGENASE HYDROXYLASE, FORM II PRESSURIZED WITH XENON GAS==
<StructureSection load='1fzh' size='340' side='right'caption='[[1fzh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fzh]] 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=1FZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FZH FirstGlance]. <br>
</td></tr><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=XE:XENON'>XE</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methane_monooxygenase_(soluble) Methane monooxygenase (soluble)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fzh OCA], [https://pdbe.org/1fzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fzh RCSB], [https://www.ebi.ac.uk/pdbsum/1fzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fzh ProSAT]</span></td></tr>
</table>
== Function ==
[[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. [[https://www.uniprot.org/uniprot/MEMG_METCA MEMG_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. [[https://www.uniprot.org/uniprot/MEMB_METCA MEMB_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. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fz/1fzh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fzh ConSurf].
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== Publication Abstract from PubMed ==
To investigate the role of protein cavities in facilitating movement of the substrates, methane and dioxygen, in the soluble methane monooxygenase hydroxylase (MMOH), we determined the X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibromomethane or iodoethane, or by using crystals pressurized with xenon gas. The halogenated alkanes bind in two cavities within the alpha-subunit that extend from one surface of the protein to the buried dinuclear iron active site. Two additional binding sites were located in the beta-subunit. Pressurization of two crystal forms of MMOH with xenon resulted in the identification of six binding sites located exclusively in the alpha-subunit. These results indicate that hydrophobic species bind preferentially in preexisting cavities in MMOH and support the hypothesis that such cavities may play a functional role in sequestering and enhancing the availability of the physiological substrates for reaction at the active site.

Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.,Whittington DA, Rosenzweig AC, Frederick CA, Lippard SJ Biochemistry. 2001 Mar 27;40(12):3476-82. PMID:11297413<ref>PMID:11297413</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1fzh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Methane monooxygenase|Methane monooxygenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylococcus capsulatus]]
[[Category: Frederick, C A]]
[[Category: Lippard, S J]]
[[Category: Rosenzweig, A C]]
[[Category: Whittington, D A]]
[[Category: Dinuclear iron center]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]