2qve: Difference between revisions
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==Crystal Structure of SgTAM bound to mechanism based inhibitor== | ==Crystal Structure of SgTAM bound to mechanism based inhibitor== | ||
<StructureSection load='2qve' size='340' side='right' caption='[[2qve]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2qve' size='340' side='right'caption='[[2qve]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qve]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_globisporus"_krasil'nikov_1941 "actinomyces globisporus" krasil'nikov 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QVE FirstGlance]. <br> | <table><tr><td colspan='2'>[[2qve]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_globisporus"_krasil'nikov_1941 "actinomyces globisporus" krasil'nikov 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QVE FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/2qve_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/2qve_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2qve" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2qve" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aminomutase 3D structures|Aminomutase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Actinomyces globisporus krasil'nikov 1941]] | [[Category: Actinomyces globisporus krasil'nikov 1941]] | ||
[[Category: Large Structures]] | |||
[[Category: Tyrosine 2,3-aminomutase]] | [[Category: Tyrosine 2,3-aminomutase]] | ||
[[Category: Bruner, S D]] | [[Category: Bruner, S D]] | ||
Revision as of 10:31, 24 July 2019
Crystal Structure of SgTAM bound to mechanism based inhibitorCrystal Structure of SgTAM bound to mechanism based inhibitor
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 PubMedThe synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM. Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM.,Montavon TJ, Christianson CV, Festin GM, Shen B, Bruner SD Bioorg Med Chem Lett. 2008 May 15;18(10):3099-102. Epub 2007 Nov 19. PMID:18078753[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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