5esh: Difference between revisions
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==Saccharomyces cerevisiae CYP51 (Lanosterol 14-alpha demethylase) G73W mutant in complex with itraconazole== | ==Saccharomyces cerevisiae CYP51 (Lanosterol 14-alpha demethylase) G73W mutant in complex with itraconazole== | ||
<StructureSection load='5esh' size='340' side='right' caption='[[5esh]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='5esh' size='340' side='right'caption='[[5esh]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5esh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ESH FirstGlance]. <br> | <table><tr><td colspan='2'>[[5esh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ESH FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Baker's yeast]] | [[Category: Baker's yeast]] | ||
[[Category: Large Structures]] | |||
[[Category: Sterol 14-demethylase]] | [[Category: Sterol 14-demethylase]] | ||
[[Category: Keniya, M V]] | [[Category: Keniya, M V]] | ||
Revision as of 11:55, 1 January 2020
Saccharomyces cerevisiae CYP51 (Lanosterol 14-alpha demethylase) G73W mutant in complex with itraconazoleSaccharomyces cerevisiae CYP51 (Lanosterol 14-alpha demethylase) G73W mutant in complex with itraconazole
Structural highlights
Publication Abstract from PubMedBitopic integral membrane proteins with a single transmembrane helix play diverse roles in catalysis, cell signaling, and morphogenesis. Complete monospanning protein structures are needed to show how interaction between the transmembrane helix and catalytic domain might influence association with the membrane and function. We report crystal structures of full-length Saccharomyces cerevisiae lanosterol 14alpha-demethylase, a membrane monospanning cytochrome P450 of the CYP51 family that catalyzes the first postcyclization step in ergosterol biosynthesis and is inhibited by triazole drugs. The structures reveal a well-ordered N-terminal amphipathic helix preceding a putative transmembrane helix that would constrain the catalytic domain orientation to lie partly in the lipid bilayer. The structures locate the substrate lanosterol, identify putative substrate and product channels, and reveal constrained interactions with triazole antifungal drugs that are important for drug design and understanding drug resistance. Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer.,Monk BC, Tomasiak TM, Keniya MV, Huschmann FU, Tyndall JD, O'Connell JD 3rd, Cannon RD, McDonald JG, Rodriguez A, Finer-Moore JS, Stroud RM Proc Natl Acad Sci U S A. 2014 Mar 11;111(10):3865-70. doi:, 10.1073/pnas.1324245111. Epub 2014 Feb 3. PMID:24613931[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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