1zb8: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1zb8.gif|left|200px]]
{{Seed}}
[[Image:1zb8.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zb8|  PDB=1zb8  |  SCENE=  }}  
{{STRUCTURE_1zb8|  PDB=1zb8  |  SCENE=  }}  


'''Crystal structure of Xylella fastidiosa organic peroxide resistance protein'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_16631787}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16631787 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16631787}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Vidigal, S A.]]
[[Category: Vidigal, S A.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:24:45 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:44:04 2008''