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2bf3

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[[Image:2bf3.gif|left|200px]]<br />
 
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<applet load="2bf3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2bf3, resolution 1.96&Aring;" />
 
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'''CRYSTAL STRUCTURE OF A TOLUENE 4-MONOOXYGENASE CATALYTIC EFFECTOR PROTEIN VARIANT MISSING TEN N-TERMINAL RESIDUES (DELTA-N10 T4MOD)'''<br />
 
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==Overview==
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==Crystal structure of a toluene 4-monooxygenase catalytic effector protein variant missing ten N-terminal residues (delta-N10 T4moD)==
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Toluene 4-monooxygenase (T4MO) is a four-component complex that catalyzes, the regiospecific, NADH-dependent hydroxylation of toluene to yield, p-cresol. The catalytic effector (T4moD) of this complex is a 102-residue, protein devoid of metals or organic cofactors. It forms a complex with the, diiron hydroxylase component (T4moH) that influences both the kinetics and, regiospecificity of catalysis. Here, we report crystal structures for, native T4moD and two engineered variants with either four (DeltaN4-) or 10, (DeltaN10-) residues removed from the N-terminal at 2.1-, 1.7-, and 1.9-A, resolution, respectively. The crystal structures have C-alpha, root-mean-squared differences of less than 0.8 A for the central core, consisting of residues 11-98, showing that alterations of the N-terminal, have little influence on the folded core of the protein. The central core, has the same fold topology as observed in the NMR structures of T4moD, the, methane monooxygenase effector protein (MmoB) from two methanotrophs, and, the phenol hydroxylase effector protein (DmpM). However, the, root-mean-squared differences between comparable C-alpha positions in the, X-ray structures and the NMR structures vary from approximately 1.8 A to, greater than 6 A. The X-ray structures exhibit an estimated overall, coordinate error from 0.095 (0.094) A based on the R-value (R free) for, the highest resolution DeltaN4-T4moD structure to 0.211 (0.196) A for the, native T4moD structure. Catalytic studies of the DeltaN4-, DeltaN7-, and, DeltaN10- variants of T4moD show statistically insignificant changes in, k(cat), K(M), k(cat)/K(M), and K(I) relative to the native protein., Moreover, there was no significant change in the regiospecificity of, toluene oxidation with any of the T4moD variants. The relative, insensitivity to changes in the N-terminal region distinguishes T4moD from, the MmoB homologues, which each require the approximately 33 residue, N-terminal region for catalytic activity.
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<StructureSection load='2bf3' size='340' side='right'caption='[[2bf3]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bf3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf3 OCA], [https://pdbe.org/2bf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bf3 RCSB], [https://www.ebi.ac.uk/pdbsum/2bf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TMOD_PSEME TMOD_PSEME] Effector protein subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. Required for optimal efficiency and specificity of the holoenzyme.<ref>PMID:11297417</ref> <ref>PMID:15882052</ref> <ref>PMID:19033467</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bf3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bf3 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2BF3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina] with HTO as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BF3 OCA].
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Crystal structures and functional studies of T4moD, the toluene 4-monooxygenase catalytic effector protein., Lountos GT, Mitchell KH, Studts JM, Fox BG, Orville AM, Biochemistry. 2005 May 17;44(19):7131-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15882052 15882052]
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__TOC__
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[[Category: Protein complex]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas mendocina]]
[[Category: Pseudomonas mendocina]]
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[[Category: Fox, B.G.]]
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[[Category: Fox BG]]
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[[Category: Lountos, G.T.]]
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[[Category: Lountos GT]]
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[[Category: Mitchell, K.H.]]
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[[Category: Mitchell KH]]
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[[Category: Orville, A.M.]]
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[[Category: Orville AM]]
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[[Category: Studts, J.M.]]
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[[Category: Studts JM]]
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[[Category: HTO]]
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[[Category: aromatic hydrocarbon catabolism]]
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[[Category: catalytic effector protein]]
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[[Category: molecular replacement]]
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[[Category: monooxygenase]]
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[[Category: n-terminal truncated mutant]]
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[[Category: oxidoreductase]]
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[[Category: toluene oxidation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:12:03 2007''
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Current revision

Crystal structure of a toluene 4-monooxygenase catalytic effector protein variant missing ten N-terminal residues (delta-N10 T4moD)

PDB ID 2bf3

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