1mmo: Difference between revisions

New page: left|200px<br /><applet load="1mmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mmo, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1mmo.gif|left|200px]]<br /><applet load="1mmo" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mmo, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE==
The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric, hydroxylase protein of methane monooxygenase from Methylococcus capsulatus, (Bath) reveals the geometry of the catalytic di-iron core. The two iron, atoms are bridged by exogenous hydroxide and acetate ligands and further, coordinated by four glutamate residues, two histidine residues and a water, molecule. The dinuclear iron centre lies in a hydrophobic active-site, cavity for binding methane. An extended canyon runs between alpha beta, pairs, which have many long alpha-helices, for possible docking of the, reductase and coupling proteins required for catalysis.
<StructureSection load='1mmo' size='340' side='right'caption='[[1mmo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mmo]] 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=1MMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMO 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</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=1mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmo OCA], [https://pdbe.org/1mmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmo RCSB], [https://www.ebi.ac.uk/pdbsum/1mmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmo 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/mm/1mmo_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=1mmo ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MMO 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 FE and ACY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MMO OCA].
*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane., Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P, Nature. 1993 Dec 9;366(6455):537-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8255292 8255292]
[[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: Nordlund P]]
[[Category: Nordlund, P.]]
[[Category: Rosenzweig AC]]
[[Category: Rosenzweig, A.C.]]
[[Category: ACY]]
[[Category: FE]]
[[Category: oxidoreductase (monooxygenase)]]
 
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