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| | ==Crystal Structure of the reduced Toluene 4-Monooxygenase HD T201A mutant complex== | | ==Crystal Structure of the reduced Toluene 4-Monooxygenase HD T201A mutant complex== |
| - | <StructureSection load='3ge3' size='340' side='right' caption='[[3ge3]], [[Resolution|resolution]] 1.52Å' scene=''> | + | <StructureSection load='3ge3' size='340' side='right'caption='[[3ge3]], [[Resolution|resolution]] 1.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ge3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25411 Atcc 25411]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GE3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ge3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25411 Atcc 25411]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GE3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dhi|3dhi]], [[3ge8|3ge8]], [[3dhh|3dhh]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dhi|3dhi]], [[3ge8|3ge8]], [[3dhh|3dhh]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmoA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411])</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=3ge3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ge3 OCA], [http://pdbe.org/3ge3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ge3 RCSB], [http://www.ebi.ac.uk/pdbsum/3ge3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ge3 ProSAT]</span></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=3ge3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ge3 OCA], [https://pdbe.org/3ge3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ge3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ge3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ge3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/TMOB_PSEME TMOB_PSEME]] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.<ref>PMID:19290655</ref> <ref>PMID:19705873</ref> [[http://www.uniprot.org/uniprot/TMOE_PSEME TMOE_PSEME]] Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. | + | [[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> [[https://www.uniprot.org/uniprot/TMOB_PSEME TMOB_PSEME]] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.<ref>PMID:19290655</ref> <ref>PMID:19705873</ref> [[https://www.uniprot.org/uniprot/TMOE_PSEME TMOE_PSEME]] Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Monooxygenase|Monooxygenase]] | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 25411]] | | [[Category: Atcc 25411]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Bailey, L J]] | | [[Category: Bailey, L J]] |
| | [[Category: Elsen, N L]] | | [[Category: Elsen, N L]] |
| Structural highlights
3ge3 is a 4 chain structure with sequence from Atcc 25411. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | |
| Gene: | tmoA (ATCC 25411), tmoE (ATCC 25411), tmoB (ATCC 25411), tmoD (ATCC 25411) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[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.[1] [2] [3] [TMOB_PSEME] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.[4] [5] [TMOE_PSEME] Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.
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 active site residue Thr-201 in toluene 4-monooxygenase hydroxylase (T4moH) has a structural counterpart in the active sites of all diiron monooxygenases. Thus, our previous finding that mutation of this residue to Ala, Gly, or Ser had no impact on steady-state catalysis or coupling was surprising. In this work, we provide kinetic, biochemical, and structural evidence that one role of Thr-201 may be to stabilize a peroxo-level intermediate during enzyme catalysis. During reactions in the absence of substrate, T201 T4moH slowly consumed O(2) but only a negligible amount of H(2)O(2) was released. In contrast, T201A T4moH gave stoichometric release of H(2)O(2) during reaction in the absence of substrate. Both enzyme isoforms were tightly coupled during steady-state catalysis with saturating toluene and other optimal substrates and exhibited near-identical kinetic parameters. However, rapid mix single-turnover studies showed that T201A T4moH had a faster first-order rate constant for product formation than T201 T4moH did. Comparison of X-ray crystal structures of resting and reduced T201A T4moH in complex with T4moD with comparable structures of T201 T4moHD revealed changes in the positions of several key active site residues relative to the comparable structures of T201 T4moH with T4moD. This combination of catalytic and structural studies offers important new insight into the role of the role of conserved Thr-201, and its contributions to the catalytic reaction cycle.
Role for threonine 201 in the catalytic cycle of the soluble diiron hydroxylase toluene 4-monooxygenase.,Elsen NL, Bailey LJ, Hauser AD, Fox BG Biochemistry. 2009 May 12;48(18):3838-46. PMID:19290655[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hemmi H, Studts JM, Chae YK, Song J, Markley JL, Fox BG. Solution structure of the toluene 4-monooxygenase effector protein (T4moD). Biochemistry. 2001 Mar 27;40(12):3512-24. PMID:11297417
- ↑ Lountos GT, Mitchell KH, Studts JM, Fox BG, Orville AM. Crystal structures and functional studies of T4moD, the toluene 4-monooxygenase catalytic effector protein. Biochemistry. 2005 May 17;44(19):7131-42. PMID:15882052 doi:10.1021/bi047459g
- ↑ Bailey LJ, McCoy JG, Phillips GN Jr, Fox BG. Structural consequences of effector protein complex formation in a diiron hydroxylase. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19194-8. Epub 2008 Nov 25. PMID:19033467
- ↑ Elsen NL, Bailey LJ, Hauser AD, Fox BG. Role for threonine 201 in the catalytic cycle of the soluble diiron hydroxylase toluene 4-monooxygenase. Biochemistry. 2009 May 12;48(18):3838-46. PMID:19290655 doi:10.1021/bi900144a
- ↑ Bailey LJ, Fox BG. Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase. Biochemistry. 2009 Sep 29;48(38):8932-9. PMID:19705873 doi:10.1021/bi901150a
- ↑ Elsen NL, Bailey LJ, Hauser AD, Fox BG. Role for threonine 201 in the catalytic cycle of the soluble diiron hydroxylase toluene 4-monooxygenase. Biochemistry. 2009 May 12;48(18):3838-46. PMID:19290655 doi:10.1021/bi900144a
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