5mi1: Difference between revisions
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==The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 9-th structure of the series with total exposition time 243 min.== | ==The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 9-th structure of the series with total exposition time 243 min.== | ||
<StructureSection load='5mi1' size='340' side='right' caption='[[5mi1]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='5mi1' size='340' side='right'caption='[[5mi1]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5mi1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Steccherinum_murashkinskyi Steccherinum murashkinskyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MI1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5mi1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Steccherinum_murashkinskyi Steccherinum murashkinskyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MI1 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5mi1" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5mi1" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Laccase]] | [[Category: Laccase]] | ||
[[Category: Large Structures]] | |||
[[Category: Steccherinum murashkinskyi]] | [[Category: Steccherinum murashkinskyi]] | ||
[[Category: Fedorova, T V]] | [[Category: Fedorova, T V]] | ||
Revision as of 15:25, 17 July 2019
The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 9-th structure of the series with total exposition time 243 min.The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 9-th structure of the series with total exposition time 243 min.
Structural highlights
Publication Abstract from PubMedThe laccase from Steccherinum murashkinskyi is a member of the large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates, accompanied by the reduction of dioxygen to water. The reducing properties of X-ray radiation and the high quality of the laccase crystals allow the study of the catalytic reduction of dioxygen to water directly in a crystal. A series of diffraction data sets with increasing absorbed radiation dose were collected from a single crystal of Steccherinum murashkinskyi laccase at 1.35 A resolution. Changes in the active-site structure associated with the reduction of molecular oxygen to water on increasing the absorbed dose of ionizing radiation were detected. The structures in the series are mixtures of different states of the enzyme-substrate complex. Nevertheless, it was possible to interpret these structures as complexes of various oxygen ligands with copper ions in different oxidation states. The results allowed the mechanism of oxygen reduction catalyzed by laccases to be refined. Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism.,Polyakov KM, Gavryushov S, Ivanova S, Fedorova TV, Glazunova OA, Popov AN, Koroleva OV Acta Crystallogr D Struct Biol. 2017 May 1;73(Pt 5):388-401. doi:, 10.1107/S2059798317003667. Epub 2017 Apr 26. PMID:28471364[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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