1mmo

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Revision as of 06:48, 29 November 2017

CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE

Structural highlights

1mmo is a 6 chain structure with sequence from Acm 1292. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Methane monooxygenase (soluble), with EC number 1.14.13.25
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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.

References

↑ Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature. 1993 Dec 9;366(6455):537-43. PMID:8255292 doi:http://dx.doi.org/10.1038/366537a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mmo"

Categories: Acm 1292 | Frederick, C A | Lippard, S J | Nordlund, P | Rosenzweig, A C

@@ Line 1: / Line 1: @@
 ==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]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
 <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>
-<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=1mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmo OCA], [http://pdbe.org/1mmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mmo RCSB], [http://www.ebi.ac.uk/pdbsum/1mmo PDBsum]</span></td></tr>
+<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=1mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmo OCA], [http://pdbe.org/1mmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mmo RCSB], [http://www.ebi.ac.uk/pdbsum/1mmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmo ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1mmo" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Methane monooxygenase|Methane monooxygenase]]
 == References ==
 <references/>

1mmo

From Proteopedia

Revision as of 06:48, 29 November 2017

CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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