4d17: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of cofactor-free urate oxidase in complex with its 5-peroxoisourate intermediate (X-ray dose, 106 kGy)== | ==Crystal structure of cofactor-free urate oxidase in complex with its 5-peroxoisourate intermediate (X-ray dose, 106 kGy)== | ||
<StructureSection load='4d17' size='340' side='right' caption='[[4d17]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='4d17' size='340' side='right'caption='[[4d17]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D17 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4d17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D17 FirstGlance]. <br> | ||
| Line 20: | Line 20: | ||
</div> | </div> | ||
<div class="pdbe-citations 4d17" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4d17" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Urate Oxidase|Urate Oxidase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 26: | Line 29: | ||
[[Category: Aspfl]] | [[Category: Aspfl]] | ||
[[Category: Factor independent urate hydroxylase]] | [[Category: Factor independent urate hydroxylase]] | ||
[[Category: Large Structures]] | |||
[[Category: Bui, S]] | [[Category: Bui, S]] | ||
[[Category: Steiner, R A]] | [[Category: Steiner, R A]] | ||
[[Category: Cofactor-free oxidase]] | [[Category: Cofactor-free oxidase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 12:51, 5 February 2020
Crystal structure of cofactor-free urate oxidase in complex with its 5-peroxoisourate intermediate (X-ray dose, 106 kGy)Crystal structure of cofactor-free urate oxidase in complex with its 5-peroxoisourate intermediate (X-ray dose, 106 kGy)
Structural highlights
Function[URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. Publication Abstract from PubMedCofactor-free oxidases and oxygenases promote and control the reactivity of O2 with limited chemical tools at their disposal. Their mechanism of action is not completely understood and structural information is not available for any of the reaction intermediates. Near-atomic resolution crystallography supported by in crystallo Raman spectroscopy and QM/MM calculations showed unambiguously that the archetypical cofactor-free uricase catalyzes uric acid degradation via a C5(S)-(hydro)peroxide intermediate. Low X-ray doses break specifically the intermediate C5OO(H) bond at 100 K, thus releasing O2 in situ, which is trapped above the substrate radical. The dose-dependent rate of bond rupture followed by combined crystallographic and Raman analysis indicates that ionizing radiation kick-starts both peroxide decomposition and its regeneration. Peroxidation can be explained by a mechanism in which the substrate radical recombines with superoxide transiently produced in the active site. Direct Evidence for a Peroxide Intermediate and a Reactive Enzyme-Substrate-Dioxygen Configuration in a Cofactor-free Oxidase.,Bui S, von Stetten D, Jambrina PG, Prange T, Colloc'h N, de Sanctis D, Royant A, Rosta E, Steiner RA Angew Chem Int Ed Engl. 2014 Oct 14. doi: 10.1002/anie.201405485. PMID:25314114[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||