1w9b: Difference between revisions
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==S. alba myrosinase in complex with carba-glucotropaeolin== | ==S. alba myrosinase in complex with carba-glucotropaeolin== | ||
<StructureSection load='1w9b' size='340' side='right' caption='[[1w9b]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1w9b' size='340' side='right'caption='[[1w9b]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1w9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sinapis_alba Sinapis alba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W9B FirstGlance]. <br> | <table><tr><td colspan='2'>[[1w9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sinapis_alba Sinapis alba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W9B FirstGlance]. <br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Sinapis alba]] | [[Category: Sinapis alba]] | ||
[[Category: Thioglucosidase]] | [[Category: Thioglucosidase]] | ||
Revision as of 14:49, 10 May 2019
S. alba myrosinase in complex with carba-glucotropaeolinS. alba myrosinase in complex with carba-glucotropaeolin
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMyrosinase, a thioglucoside glucohydrolase, is the only enzyme able to hydrolyse glucosinolates, a unique family of molecules bearing an anomeric O-sulfated thiohydroximate function. Non-hydrolysable myrosinase inhibitors have been devised and studied for their biological interaction. Diverse modifications of the O-sulfate moiety did not result in a significant inhibitory effect, whereas replacing the D-glucopyrano residue by its carba-analogue allowed inhibition to take place. X-Ray experiments carried out after soaking allowed for the first time inclusion of a non-hydrolysable inhibitor inside the enzymatic pocket. Structural tuning of the aglycon part in its pocket is being used as a guide for the development of simplified and more potent inhibitors. The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors.,Bourderioux A, Lefoix M, Gueyrard D, Tatibouet A, Cottaz S, Arzt S, Burmeister WP, Rollin P Org Biomol Chem. 2005 May 21;3(10):1872-9. Epub 2005 Apr 14. PMID:15889170[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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