2cjc: Difference between revisions
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==Complexes of Dodecin with Flavin and Flavin-like Ligands== | ==Complexes of Dodecin with Flavin and Flavin-like Ligands== | ||
<StructureSection load='2cjc' size='340' side='right' caption='[[2cjc]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2cjc' size='340' side='right'caption='[[2cjc]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cjc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2cjc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJC FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus halobius ruber klebahn 1919]] | [[Category: Bacillus halobius ruber klebahn 1919]] | ||
[[Category: Large Structures]] | |||
[[Category: Grininger, M]] | [[Category: Grininger, M]] | ||
[[Category: Oesterhelt, D]] | [[Category: Oesterhelt, D]] | ||
Revision as of 13:57, 26 February 2020
Complexes of Dodecin with Flavin and Flavin-like LigandsComplexes of Dodecin with Flavin and Flavin-like Ligands
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 PubMedBoth extensive theoretical calculations and experimental data obtained during several decades leave little doubt that flavin adenine dinucleotide (FAD) exists in an open as well as in a closed conformation in aqueous solution. However, the knowledge about the intramolecularly stacked complex of FAD is constructed on indirect methods while direct structural evidence is lacking. Recently, dodecin was reported as an unspecific flavin binding protein which exhibits the unique binding mode of incorporating stacked dimers of flavins into a single binding pocket. Here, we show that FAD is not bound in this manner, but in monomers of intramolecularly stacked conformation. As resulting from the dodecin ligand binding characteristic, this FAD stacked conformation suggests to be directly sequestered from the aqueous solution and thus to be the first X-ray structural view on a FAD solution-stacked form. Moreover, in extraordinary FAD binding, dodecin serves as a model for studying bound monomeric (FAD) versus bound dimeric (e.g. riboflavin) flavin properties. Dodecin sequesters FAD in closed conformation from the aqueous solution.,Grininger M, Seiler F, Zeth K, Oesterhelt D J Mol Biol. 2006 Dec 8;364(4):561-6. Epub 2006 Sep 5. PMID:17027852[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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