1fz8: Difference between revisions

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-[[Image:1fz8.gif|left|200px]]<br /><applet load="1fz8" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1fz8, resolution 2.10&Aring;" />
-'''METHANE MONOOXYGENASE HYDROXYLASE, FORM II COCRYSTALLIZED WITH DIBROMOMETHANE'''<br />
-==Overview==
+==METHANE MONOOXYGENASE HYDROXYLASE, FORM II COCRYSTALLIZED WITH DIBROMOMETHANE==
-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='1fz8' size='340' side='right'caption='[[1fz8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fz8]] 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=1FZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FZ8 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]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BM:DIBROMOMETHANE'>2BM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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=1fz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fz8 OCA], [https://pdbe.org/1fz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fz8 RCSB], [https://www.ebi.ac.uk/pdbsum/1fz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fz8 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/1fz8_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=1fz8 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FZ8 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>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=2BM:'>2BM</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=1FZ8 OCA].
+*[[Methane monooxygenase|Methane monooxygenase]]
+*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
-==Reference==
+__TOC__
-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]
+</StructureSection>
-[[Category: Methane monooxygenase]]
+[[Category: Large Structures]]
 [[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: 2BM]]
-[[Category: CA]]
-[[Category: FE]]
-[[Category: dinuclear iron center]]
-[[Category: monooxygenase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:15 2008''