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| | ==METHANE MONOOXYGENASE COMPONENT B== | | ==METHANE MONOOXYGENASE COMPONENT B== |
| - | <StructureSection load='2mob' size='340' side='right' caption='[[2mob]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2mob' size='340' side='right'caption='[[2mob]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mob]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acm_3311 Acm 3311]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MOB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mob]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylosinus_trichosporium Methylosinus trichosporium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MOB FirstGlance]. <br> |
| - | </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=2mob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mob OCA], [http://pdbe.org/2mob PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mob RCSB], [http://www.ebi.ac.uk/pdbsum/2mob PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mob OCA], [https://pdbe.org/2mob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mob RCSB], [https://www.ebi.ac.uk/pdbsum/2mob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mob ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MMOB_METTR MMOB_METTR]] 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. | + | [https://www.uniprot.org/uniprot/MMOB_METTR MMOB_METTR] 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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/2mob_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/2mob_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 2mob" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2mob" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acm 3311]] | + | [[Category: Large Structures]] |
| - | [[Category: Chang, S L]] | + | [[Category: Methylosinus trichosporium]] |
| - | [[Category: Lipscomb, J D]] | + | [[Category: Chang SL]] |
| - | [[Category: Mayo, K H]] | + | [[Category: Lipscomb JD]] |
| - | [[Category: Wallar, B J]] | + | [[Category: Mayo KH]] |
| - | [[Category: Methane oxidation]] | + | [[Category: Wallar BJ]] |
| - | [[Category: Monooxygenase]]
| + | |
| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
MMOB_METTR 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.
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
Methane monooxygenase (MMO) is a nonheme iron-containing enzyme which consists of three protein components: a hydroxylase (MMOH), an NADH-linked reductase (MMOR), and a small "B" component (MMOB) which plays a regulatory role. Here, 1H, 13C, 15N heteronuclear 2D and 3D NMR spectroscopy has been used to derive the solution structure of the 138 amino acid MMOB protein in the monomer state. Pulse field gradient NMR self-diffusion measurements indicate predominant formation of dimers at 1 mM MMOB and monomers at or below 0.2 mM. MMOB is active as a monomer. Aggregate exchange broadening and limited solubility dictated that multidimensional heteronuclear NMR experiments had to be performed at a protein concentration of 0.2 mM. Using 1340 experimental constraints (1182 NOEs, 98 dihedrals, and 60 hydrogen bonding) within the well-folded part of the protein (residues 36-126), MMOB structural modeling produced a well-defined, compact alpha/beta fold which consists of three alpha-helices and six antiparallel beta-strands arranged in two domains: a betaalphabetabeta and a betaalphaalphabetabeta. Excluding the ill-defined N- and C-terminal segments (residues 1-35 and 127-138), RMS deviations are 1.1 A for backbone atoms and 1.6 A for all non-hydrogen atoms. Compared to the lower resolution NMR structure for the homologous protein P2 from the Pseudomonas sp. CF600 phenol hydroxylase system (RMSD = 2.48 A for backbone atoms) (Qian, H., Edlund, U., Powlowski, J., Shingler, V., and Sethson, I. (1997) Biochemistry, 36, 495-504), that of MMOB reveals a considerably more compact protein. In particular, MMOB lacks the large "doughnut" shaped cavity reported for the P2 protein. This difference may result from the limited number of long-range NOEs that were available for use in the modeling of the P2 structure. This NMR-derived structure of MMOB, therefore, presents the first high-resolution structure of a small protein effector of a nonheme oxygenase system.
Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.,Chang SL, Wallar BJ, Lipscomb JD, Mayo KH Biochemistry. 1999 May 4;38(18):5799-812. PMID:10231531[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chang SL, Wallar BJ, Lipscomb JD, Mayo KH. Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. Biochemistry. 1999 May 4;38(18):5799-812. PMID:10231531 doi:10.1021/bi982992f
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