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[[Image:1fzi.gif|left|200px]]<br /><applet load="1fzi" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fzi, resolution 3.30&Aring;" />
'''METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS'''<br />


==Overview==
==METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS==
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.
<StructureSection load='1fzi' size='340' side='right'caption='[[1fzi]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fzi]] 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=1FZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FZI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></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=1fzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fzi OCA], [https://pdbe.org/1fzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fzi RCSB], [https://www.ebi.ac.uk/pdbsum/1fzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fzi 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.
== 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/1fzi_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=1fzi ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FZI 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=XE:'>XE</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=1FZI OCA].
*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11297413 11297413]
[[Category: Large Structures]]
[[Category: Methane monooxygenase]]
[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
[[Category: Protein complex]]
[[Category: Frederick CA]]
[[Category: Frederick, C A.]]
[[Category: Lippard SJ]]
[[Category: Lippard, S J.]]
[[Category: Rosenzweig AC]]
[[Category: Rosenzweig, A C.]]
[[Category: Whittington DA]]
[[Category: Whittington, D A.]]
[[Category: FE]]
[[Category: XE]]
[[Category: dinuclear iron center]]
[[Category: monooxygenase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:19 2008''

Latest revision as of 10:20, 7 February 2024

METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GASMETHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS

Structural highlights

1fzi is a 6 chain structure with sequence from Methylococcus capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1fzi, resolution 3.30Å

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