View source for 2mob


==METHANE MONOOXYGENASE COMPONENT B==
<StructureSection load='2mob' size='340' side='right'caption='[[2mob]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mob]] is a 1 chain structure with sequence from [https://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 [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'>[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>
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== Function ==
[[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <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>
    <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=2mob ConSurf].
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== 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<ref>PMID:10231531</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Methane monooxygenase|Methane monooxygenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acm 3311]]
[[Category: Large Structures]]
[[Category: Chang, S L]]
[[Category: Lipscomb, J D]]
[[Category: Mayo, K H]]
[[Category: Wallar, B J]]
[[Category: Methane oxidation]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]