From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2e3t.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2e3t.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2e3t| PDB=2e3t | SCENE= }} | | {{STRUCTURE_2e3t| PDB=2e3t | SCENE= }} |
| | | | |
| - | '''Crystal structure of rat xanthine oxidoreductase mutant (W335A and F336L)'''
| + | ===Crystal structure of rat xanthine oxidoreductase mutant (W335A and F336L)=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Reactive oxygen species are generated by various systems, including NADPH oxidases, xanthine oxidoreductase (XOR) and mitochondrial respiratory enzymes, and contribute to many physiological and pathological phenomena. Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide in a molar ratio of about 1:3, depending upon the conditions. Here, we present a mutant of rat XOR that displays mainly XO activity with a superoxide:hydrogen peroxide production ratio of about 6:1. In the mutant, tryptophan 335, which is a component of the amino acid cluster crucial for switching from the XDH to the XO conformation, was replaced with alanine, and phenylalanine 336, which modulates FAD's redox potential through stacking interactions with the flavin cofactor, was changed to leucine. When the mutant was expressed in Sf9 cells, it was obtained in the XO form, and dithiothreitol treatment only partially restored the pyridine nucleotide-binding capacity. The crystal structure of the dithiothreitol-treated mutant at 2.3 Angstroms resolution showed the enzyme's two subunits to be quite similar, but not identical: the cluster involved in conformation-switching was completely disrupted in one subunit, but remained partly associated in the other one. The chain trace of the active site loop in this mutant is very similar to that of the bovine XO form. These results are consistent with the idea that the XDH and XO forms of the mutant are in an equilibrium that greatly favours the XO form, but the equilibrium is partly shifted towards the XDH form upon incubation with dithiothreitol.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17301076}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17301076 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17301076}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Dehydrogenase to oxidase conversion]] | | [[Category: Dehydrogenase to oxidase conversion]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:52:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:25:29 2008'' |
Revision as of 10:25, 29 July 2008
Template:STRUCTURE 2e3t
Crystal structure of rat xanthine oxidoreductase mutant (W335A and F336L)
Template:ABSTRACT PUBMED 17301076
About this Structure
2E3T is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase., Asai R, Nishino T, Matsumura T, Okamoto K, Igarashi K, Pai EF, Nishino T, J Biochem. 2007 Apr;141(4):525-34. Epub 2007 Feb 14. PMID:17301076
Page seeded by OCA on Tue Jul 29 13:25:29 2008
