1vm9
From Proteopedia
(New page: 200px<br /><applet load="1vm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vm9, resolution 1.480Å" /> '''The X-ray Structure...) |
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| - | [[Image:1vm9.gif|left|200px]]<br /><applet load="1vm9" size=" | + | [[Image:1vm9.gif|left|200px]]<br /><applet load="1vm9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vm9, resolution 1.480Å" /> | caption="1vm9, resolution 1.480Å" /> | ||
'''The X-ray Structure of the cys84ala cys85ala double mutant of the [2Fe-2S] Ferredoxin subunit of Toluene-4-Monooxygenase from Pseudomonas Mendocina KR1'''<br /> | '''The X-ray Structure of the cys84ala cys85ala double mutant of the [2Fe-2S] Ferredoxin subunit of Toluene-4-Monooxygenase from Pseudomonas Mendocina KR1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the Rieske-type ferredoxin (T4moC) from toluene | + | The structure of the Rieske-type ferredoxin (T4moC) from toluene 4-monooxygenase was determined by X-ray crystallography in the [2Fe-2S](2+) state at a resolution of 1.48 A using single-wavelength anomalous dispersion phasing with the [2Fe-2S] center. The structure consists of ten beta-strands arranged into the three antiparallel beta-sheet topology observed in all Rieske proteins. Trp69 of T4moC is adjacent to the [2Fe-2S] centre, which displaces a loop containing the conserved Pro81 by approximately 8 A away from the [2Fe-2S] cluster compared with the Pro loop in the closest structural and functional homolog, the Rieske-type ferredoxin BphF from biphenyl dioxygenase. In addition, T4moC contains five hydrogen bonds to the [2Fe-2S] cluster compared with three hydrogen bonds in BphF. Moreover, the electrostatic surface of T4moC is distinct from that of BphF. These structural differences are identified as possible contributors to the evolutionary specialization of soluble Rieske-type ferredoxins between the diiron monooxygenases and cis-dihydrodiol-forming dioxygenases. |
==About this Structure== | ==About this Structure== | ||
| - | 1VM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina] with MG, FES and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1VM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas mendocina]] | [[Category: Pseudomonas mendocina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Allard, S | + | [[Category: Allard, S T.M.]] |
| - | [[Category: Bingman, C | + | [[Category: Bingman, C A.]] |
| - | [[Category: CESG, Center | + | [[Category: CESG, Center for Eukaryotic Structural Genomics.]] |
| - | [[Category: Fox, B | + | [[Category: Fox, B G.]] |
| - | [[Category: Jr., G | + | [[Category: Jr., G N.Phillips.]] |
| - | [[Category: Moe, L | + | [[Category: Moe, L A.]] |
| - | [[Category: Smith, D | + | [[Category: Smith, D W.]] |
| - | [[Category: Wesenberg, G | + | [[Category: Wesenberg, G E.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: FES]] | [[Category: FES]] | ||
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[[Category: toluene-4-monooxygenase subunit]] | [[Category: toluene-4-monooxygenase subunit]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:47 2008'' |
Revision as of 13:36, 21 February 2008
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The X-ray Structure of the cys84ala cys85ala double mutant of the [2Fe-2S] Ferredoxin subunit of Toluene-4-Monooxygenase from Pseudomonas Mendocina KR1
Overview
The structure of the Rieske-type ferredoxin (T4moC) from toluene 4-monooxygenase was determined by X-ray crystallography in the [2Fe-2S](2+) state at a resolution of 1.48 A using single-wavelength anomalous dispersion phasing with the [2Fe-2S] center. The structure consists of ten beta-strands arranged into the three antiparallel beta-sheet topology observed in all Rieske proteins. Trp69 of T4moC is adjacent to the [2Fe-2S] centre, which displaces a loop containing the conserved Pro81 by approximately 8 A away from the [2Fe-2S] cluster compared with the Pro loop in the closest structural and functional homolog, the Rieske-type ferredoxin BphF from biphenyl dioxygenase. In addition, T4moC contains five hydrogen bonds to the [2Fe-2S] cluster compared with three hydrogen bonds in BphF. Moreover, the electrostatic surface of T4moC is distinct from that of BphF. These structural differences are identified as possible contributors to the evolutionary specialization of soluble Rieske-type ferredoxins between the diiron monooxygenases and cis-dihydrodiol-forming dioxygenases.
About this Structure
1VM9 is a Single protein structure of sequence from Pseudomonas mendocina with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of T4moC, the Rieske-type ferredoxin component of toluene 4-monooxygenase., Moe LA, Bingman CA, Wesenberg GE, Phillips GN Jr, Fox BG, Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):476-82. Epub 2006, Apr 19. PMID:16627939[[Category: [2fe-2s] cluster]]
Page seeded by OCA on Thu Feb 21 15:36:47 2008
Categories: Pseudomonas mendocina | Single protein | Allard, S T.M. | Bingman, C A. | CESG, Center for Eukaryotic Structural Genomics. | Fox, B G. | Jr., G N.Phillips. | Moe, L A. | Smith, D W. | Wesenberg, G E. | EDO | FES | MG | Center for eukaryotic structural genomics | Cesg | Ferredoxin | Fes | Protein structure initiative | Psi | Rieske protein | Structural genomics | Toluene-4-monooxygenase subunit
