1qsr: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1qsr.gif|left|200px]] | [[Image:1qsr.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1qsr", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1qsr| PDB=1qsr | SCENE= }} | |||
}} | |||
'''CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A''' | '''CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A''' | ||
| Line 33: | Line 30: | ||
[[Category: Trievel, R C.]] | [[Category: Trievel, R C.]] | ||
[[Category: Zhou, J.]] | [[Category: Zhou, J.]] | ||
[[Category: | [[Category: Coa-binding protein]] | ||
[[Category: | [[Category: Gcn5-related n-acetyltransferase]] | ||
[[Category: | [[Category: Histone acetyltransferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:39:54 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:39, 3 May 2008
CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A
Overview
Gene 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.
About this Structure
1QSR is a Single protein structure of sequence from Tetrahymena thermophila. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 06:39:54 2008
