4gam

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{{Large structure}}
==Complex structure of Methane monooxygenase hydroxylase and regulatory subunit==
==Complex structure of Methane monooxygenase hydroxylase and regulatory subunit==
<StructureSection load='4gam' size='340' side='right' caption='[[4gam]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='4gam' size='340' side='right' caption='[[4gam]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gam]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] and [http://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._bath Methylococcus capsulatus str. bath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GAM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GAM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gam]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Metca Metca] and [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GAM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GAM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mmo|1mmo]], [[1ckv|1ckv]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mmo|1mmo]], [[1ckv|1ckv]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mmoB, MCA1196 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243233 Methylococcus capsulatus str. Bath])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mmoB, MCA1196 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243233 METCA])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methane_monooxygenase_(soluble) Methane monooxygenase (soluble)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gam OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gam RCSB], [http://www.ebi.ac.uk/pdbsum/4gam PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gam OCA], [http://pdbe.org/4gam PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gam RCSB], [http://www.ebi.ac.uk/pdbsum/4gam PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gam ProSAT]</span></td></tr>
</table>
</table>
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{{Large structure}}
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MMOB_METCA MMOB_METCA]] The B protein acts as a regulator of electron flow through the soluble mmo complex, switching the enzyme from an oxidase to a hydroxylase in the presence of the substrate. [[http://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. [[http://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. [[http://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.
[[http://www.uniprot.org/uniprot/MMOB_METCA MMOB_METCA]] The B protein acts as a regulator of electron flow through the soluble mmo complex, switching the enzyme from an oxidase to a hydroxylase in the presence of the substrate. [[http://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. [[http://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. [[http://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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4gam" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Methane monooxygenase]]
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[[Category: Metca]]
[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
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[[Category: Methylococcus capsulatus str. bath]]
 
[[Category: Cho, U S]]
[[Category: Cho, U S]]
[[Category: Lee, S J]]
[[Category: Lee, S J]]
[[Category: Lippard, S J]]
[[Category: Lippard, S J]]
[[Category: Hydroxylase]]
[[Category: Hydroxylase]]
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[[Category: Methane monooxygenase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Regulatory subunit b]]
[[Category: Regulatory subunit b]]

Revision as of 15:17, 4 August 2016

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Complex structure of Methane monooxygenase hydroxylase and regulatory subunit

4gam, resolution 2.90Å

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