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3dhh

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Revision as of 13:39, 24 December 2014

Crystal Structure of Resting State Toluene 4-Monoxygenase Hydroxylase Complexed with Effector Protein

Structural highlights

3dhh is a 4 chain structure with sequence from Pseudomonas mendocina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Gene:	tmoA (Pseudomonas mendocina), tmoE (Pseudomonas mendocina), tmoB (Pseudomonas mendocina), tmoD (Pseudomonas mendocina)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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]

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

Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 A from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases.

Structural consequences of effector protein complex formation in a diiron hydroxylase.,Bailey LJ, McCoy JG, Phillips GN Jr, Fox BG Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19194-8. Epub 2008 Nov 25. PMID:19033467^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ 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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dhh"

@@ Line 7: / Line 7: @@
 <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=3dhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dhh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dhh RCSB], [http://www.ebi.ac.uk/pdbsum/3dhh PDBsum]</span></td></tr>
 </table>
+== 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3dhh

From Proteopedia

Revision as of 13:39, 24 December 2014

Crystal Structure of Resting State Toluene 4-Monoxygenase Hydroxylase Complexed with Effector Protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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