This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1qsm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qsm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qsm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qsm| PDB=1qsm | SCENE= }}
{{STRUCTURE_1qsm| PDB=1qsm | SCENE= }}
-
'''HISTONE ACETYLTRANSFERASE HPA2 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A'''
+
===HISTONE ACETYLTRANSFERASE HPA2 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A===
-
==Overview==
+
<!--
-
We report the crystal structure of the yeast protein Hpa2 in complex with acetyl coenzyme A (AcCoA) at 2.4 A resolution and without cofactor at 2.9 A resolution. Hpa2 is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, a family of enzymes with diverse substrates including histones, other proteins, arylalkylamines and aminoglycosides. In vitro, Hpa2 is able to acetylate specific lysine residues of histones H3 and H4 with a preference for Lys14 of histone H3. Hpa2 forms a stable dimer in solution and forms a tetramer upon binding AcCoA. The crystal structure reveals that the Hpa2 tetramer is stabilized by base-pair interactions between the adenine moieties of the bound AcCoA molecules. These base-pairs represent a novel method of stabilizing an oligomeric protein structure. Comparison of the structure of Hpa2 with those of other GNAT superfamily members illustrates a remarkably conserved fold of the catalytic domain of the GNAT family even though members of this family share low levels of sequence homology. This comparison has allowed us to better define the borders of the four sequence motifs that characterize the GNAT family, including a motif that is not discernable in histone acetyltransferases by sequence comparison alone. We discuss implications of the Hpa2 structure for the catalytic mechanism of the GNAT enzymes and the opportunity for multiple histone tail modification created by the tetrameric Hpa2 structure.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10600387}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10600387 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10600387}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Acetyltransferase]]
[[Category: Acetyltransferase]]
[[Category: Protein-acetyl coenzyme a complex]]
[[Category: Protein-acetyl coenzyme a complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:39:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:06:16 2008''

Revision as of 09:06, 29 July 2008

Image:1qsm.png

Template:STRUCTURE 1qsm

HISTONE ACETYLTRANSFERASE HPA2 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A

Template:ABSTRACT PUBMED 10600387

About this Structure

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

Reference

Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily., Angus-Hill ML, Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V, J Mol Biol. 1999 Dec 17;294(5):1311-25. PMID:10600387

Page seeded by OCA on Tue Jul 29 12:06:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qsm"
Personal tools