1q17: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1q17.gif|left|200px]]
{{Seed}}
[[Image:1q17.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q17|  PDB=1q17  |  SCENE=  }}  
{{STRUCTURE_1q17|  PDB=1q17  |  SCENE=  }}  


'''Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide'''
===Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide===




==Overview==
<!--
Sir2 proteins are NAD(+)-dependant protein deactylases that have been implicated in playing roles in gene silencing, DNA repair, genome stability, longevity, metabolism, and cell physiology. To define the mechanism of Sir2 activity, we report the 1.5 A crystal structure of the yeast Hst2 (yHst2) Sir2 protein in ternary complex with 2'-O-acetyl ADP ribose and an acetylated histone H4 peptide. The structure captures both ligands meeting within an enclosed tunnel between the small and large domains of the catalytic protein core and permits the assignment of a detailed catalytic mechanism for the Sir2 proteins that is consistent with solution and enzymatic studies. Comparison of the ternary complex with the yHst2/NAD(+) complex, also reported here, and nascent yHst2 structure also reveals that NAD(+) binding accompanies intramolecular loop rearrangement for more stable NAD(+) and acetyl-lysine binding, and that acetyl-lysine peptide binding induces a trimer-monomer protein transition involving nonconserved Sir2 residues.
The line below this paragraph, {{ABSTRACT_PUBMED_14604530}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14604530 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_14604530}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Zhao, K.]]
[[Category: Zhao, K.]]
[[Category: Histone deacetylase]]
[[Category: Histone deacetylase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:44:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:18:37 2008''

Revision as of 12:18, 28 July 2008

File:1q17.png

Template:STRUCTURE 1q17

Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide

Template:ABSTRACT PUBMED 14604530

About this Structure

1Q17 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide., Zhao K, Chai X, Marmorstein R, Structure. 2003 Nov;11(11):1403-11. PMID:14604530

Page seeded by OCA on Mon Jul 28 15:18:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1q17&oldid=704542"