Structure and Mechanism of Action of the Histone Acetyltransferase Gcn5 and Similarity to Other N-Acetyltransferases

In this issue of the "Proceedings," Trievel et al report the crystal structure of the catalytic HAT domain of yeast GCN5. This domain encompasses residues 99-262 of the 439-aa protein.

Saved in:
Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 96; no. 16; pp. 8807 - 8808
Main Authors Sternglanz, Rolf, Schindelin, Hermann
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 03.08.1999
National Acad Sciences
National Academy of Sciences
The National Academy of Sciences
Subjects
Acetylation
Acetyltransferases - chemistry
Acetyltransferases - metabolism
Animals
Catalysis
Commentary
Conserved Sequence
Crystallography
DNA-Binding Proteins
Enzyme substrates
Enzymes
Fungal Proteins - chemistry
Fungal Proteins - metabolism
Genes
Histone Acetyltransferases
Histones
Nucleosomes
Protein Conformation
Protein Kinases - chemistry
Protein Kinases - metabolism
Protein Structure, Secondary
Proteins
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
Yeast
Yeasts
Online AccessGet full text

Cover

More Information
Summary:In this issue of the "Proceedings," Trievel et al report the crystal structure of the catalytic HAT domain of yeast GCN5. This domain encompasses residues 99-262 of the 439-aa protein.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Commentary-2
ObjectType-Feature-4
ObjectType-Review-1
ObjectType-Article-3
To whom reprint requests should be addressed. E-mail: rolf@life.bio.sunysb.edu.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.96.16.8807