1mmo: Difference between revisions
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==CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE== | ==CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE== | ||
<StructureSection load='1mmo' size='340' side='right' caption='[[1mmo]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1mmo' size='340' side='right'caption='[[1mmo]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mmo]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Acm_1292 Acm 1292]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MMO FirstGlance]. <br> | <table><tr><td colspan='2'>[[1mmo]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Acm_1292 Acm 1292]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MMO FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mmo_consurf.spt"</scriptWhenChecked> | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1mmo" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1mmo" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Methane monooxygenase|Methane monooxygenase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Acm 1292]] | [[Category: Acm 1292]] | ||
[[Category: Large Structures]] | |||
[[Category: Frederick, C A]] | [[Category: Frederick, C A]] | ||
[[Category: Lippard, S J]] | [[Category: Lippard, S J]] | ||
[[Category: Nordlund, P]] | [[Category: Nordlund, P]] | ||
[[Category: Rosenzweig, A C]] | [[Category: Rosenzweig, A C]] | ||
Revision as of 21:36, 20 November 2019
CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANECRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE
Structural highlights
Function[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. [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. [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. Publication Abstract from PubMedThe 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. 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:8255292[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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