3ge8

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[[Image:3ge8.png|left|200px]]
 
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{{STRUCTURE_3ge8| PDB=3ge8 | SCENE= }}
{{STRUCTURE_3ge8| PDB=3ge8 | SCENE= }}
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===Toluene 4-monooxygenase HD T201A diferric, resting state complex===
===Toluene 4-monooxygenase HD T201A diferric, resting state complex===
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{{ABSTRACT_PUBMED_19290655}}
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==Function==
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[[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.
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{{ABSTRACT_PUBMED_19290655}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:019290655</ref><references group="xtra"/>
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<ref group="xtra">PMID:019290655</ref><references group="xtra"/><references/>
[[Category: Pseudomonas mendocina]]
[[Category: Pseudomonas mendocina]]
[[Category: Bailey, L J.]]
[[Category: Bailey, L J.]]

Revision as of 09:40, 27 March 2013

Template:STRUCTURE 3ge8

Contents

Toluene 4-monooxygenase HD T201A diferric, resting state complex

Template:ABSTRACT PUBMED 19290655

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.

About this Structure

3ge8 is a 8 chain structure with sequence from Pseudomonas mendocina. Full crystallographic information is available from OCA.

Reference

  • 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
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

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