1zb8
From Proteopedia
(New page: 200px<br /><applet load="1zb8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zb8, resolution 2.40Å" /> '''Crystal structure of...) |
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| - | [[Image:1zb8.gif|left|200px]]<br /><applet load="1zb8" size=" | + | [[Image:1zb8.gif|left|200px]]<br /><applet load="1zb8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zb8, resolution 2.40Å" /> | caption="1zb8, resolution 2.40Å" /> | ||
'''Crystal structure of Xylella fastidiosa organic peroxide resistance protein'''<br /> | '''Crystal structure of Xylella fastidiosa organic peroxide resistance protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Organic hydroperoxide resistance proteins (Ohr) belong to a family of | + | Organic hydroperoxide resistance proteins (Ohr) belong to a family of proteins that possess thiol-dependent peroxidase activity endowed by reactive cysteine residues able to reduce peroxides. The crystal structure of Ohr from Xylella fastidiosa in complex with polyethylene glycol, providing insights into enzyme-substrate interactions is described herein. In addition, crystallographic studies, molecular modeling and biochemical assays also indicated that peroxides derived from long chain fatty acids could be the biological substrates of Ohr. Because different oxidation states of the reactive cysteine were present in the Ohr structures from X. fastidiosa, Pseudomonas aeruginosa and Deinococcus radiodurans it was possible to envisage a set of snapshots along the coordinate of the enzyme-catalyzed reaction. The redox intermediates of X. fastidiosa Ohr observed in the crystals were further characterized in solution by electrospray ionization mass spectrometry and by biochemical approaches. In this study, the formation of an intramolecular disulfide bond and oxidative inactivation through the formation of a sulfonic acid derivative was unequivocally demonstrated for the first time. Because Ohr proteins are exclusively present in bacteria, they may represent promising targets for therapeutical drugs. In this regard, the structural and functional analyses of Ohr presented here might be very useful. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xylella_fastidiosa_9a5c Xylella fastidiosa 9a5c] with PE4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xylella_fastidiosa_9a5c Xylella fastidiosa 9a5c] with <scene name='pdbligand=PE4:'>PE4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZB8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xylella fastidiosa 9a5c]] | [[Category: Xylella fastidiosa 9a5c]] | ||
| - | [[Category: Cussiol, J | + | [[Category: Cussiol, J R.]] |
| - | [[Category: Gozzo, F | + | [[Category: Gozzo, F C.]] |
| - | [[Category: Guimaraes, B | + | [[Category: Guimaraes, B G.]] |
| - | [[Category: Medrano, F | + | [[Category: Medrano, F J.]] |
| - | [[Category: Netto, L | + | [[Category: Netto, L E.]] |
| - | [[Category: Oliveira, M | + | [[Category: Oliveira, M A.]] |
| - | [[Category: Vidigal, S | + | [[Category: Vidigal, S A.]] |
[[Category: PE4]] | [[Category: PE4]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:50 2008'' |
Revision as of 14:13, 21 February 2008
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Crystal structure of Xylella fastidiosa organic peroxide resistance protein
Overview
Organic hydroperoxide resistance proteins (Ohr) belong to a family of proteins that possess thiol-dependent peroxidase activity endowed by reactive cysteine residues able to reduce peroxides. The crystal structure of Ohr from Xylella fastidiosa in complex with polyethylene glycol, providing insights into enzyme-substrate interactions is described herein. In addition, crystallographic studies, molecular modeling and biochemical assays also indicated that peroxides derived from long chain fatty acids could be the biological substrates of Ohr. Because different oxidation states of the reactive cysteine were present in the Ohr structures from X. fastidiosa, Pseudomonas aeruginosa and Deinococcus radiodurans it was possible to envisage a set of snapshots along the coordinate of the enzyme-catalyzed reaction. The redox intermediates of X. fastidiosa Ohr observed in the crystals were further characterized in solution by electrospray ionization mass spectrometry and by biochemical approaches. In this study, the formation of an intramolecular disulfide bond and oxidative inactivation through the formation of a sulfonic acid derivative was unequivocally demonstrated for the first time. Because Ohr proteins are exclusively present in bacteria, they may represent promising targets for therapeutical drugs. In this regard, the structural and functional analyses of Ohr presented here might be very useful.
About this Structure
1ZB8 is a Single protein structure of sequence from Xylella fastidiosa 9a5c with as ligand. Full crystallographic information is available from OCA.
Reference
Structural insights into enzyme-substrate interaction and characterization of enzymatic intermediates of organic hydroperoxide resistance protein from Xylella fastidiosa., Oliveira MA, Guimaraes BG, Cussiol JR, Medrano FJ, Gozzo FC, Netto LE, J Mol Biol. 2006 Jun 2;359(2):433-45. Epub 2006 Apr 7. PMID:16631787
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