1qsr: Difference between revisions
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==CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A== | ==CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A== | ||
<StructureSection load='1qsr' size='340' side='right' caption='[[1qsr]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1qsr' size='340' side='right'caption='[[1qsr]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qsr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tetth Tetth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QSR FirstGlance]. <br> | <table><tr><td colspan='2'>[[1qsr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tetth Tetth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QSR FirstGlance]. <br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Tetth]] | [[Category: Tetth]] | ||
[[Category: Allis, C David]] | [[Category: Allis, C David]] | ||
Revision as of 14:11, 4 December 2019
CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME ACRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A
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 PubMedGene activation is a highly regulated process that requires the coordinated action of proteins to relieve chromatin repression and to promote transcriptional activation. Nuclear histone acetyltransferase (HAT) enzymes provide a mechanistic link between chromatin destabilization and gene activation by acetylating the epsilon-amino group of specific lysine residues within the aminoterminal tails of core histones to facilitate access to DNA by transcriptional activators. Here we report the high-resolution crystal structure of the HAT domain of Tetrahymena GCN5 (tGCN5) bound with both its physiologically relevant ligands, coenzyme A (CoA) and a histone H3 peptide, and the structures of nascent tGCN5 and a tGCN5/acetyl-CoA complex. Our structural data reveal histone-binding specificity for a random-coil structure containing a G-K-X-P recognition sequence, and show that CoA is essential for reorienting the enzyme for histone binding. Catalysis appears to involve water-mediated proton extraction from the substrate lysine by a glutamic acid general base and a backbone amide that stabilizes the transition-state reaction intermediate. Comparison with related N-acetyltransferases indicates a conserved structural framework for CoA binding and catalysis, and structural variability in regions associated with substrate-specific binding. Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide.,Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R Nature. 1999 Sep 2;401(6748):93-8. PMID:10485713[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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