PMID- 10393169
OWN - NLM
STAT- MEDLINE
DCOM- 19990831
LR  - 20161019
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 13
DP  - 1999 Jul 1
TI  - Crystal structure of the histone acetyltransferase domain of the human PCAF
      transcriptional regulator bound to coenzyme A.
PG  - 3521-32
AB  - The human p300/CBP-associating factor, PCAF, mediates transcriptional activation 
      through its ability to acetylate nucleosomal histone substrates as well as
      transcriptional activators such as p53. We have determined the 2.3 A crystal
      structure of the histone acetyltransferase (HAT) domain of PCAF bound to coenzyme
      A. The structure reveals a central protein core associated with coenzyme A
      binding and a pronounced cleft that sits over the protein core and is flanked on 
      opposite sides by the N- and C-terminal protein segments. A correlation of the
      structure with the extensive mutagenesis data for PCAF and the homologous yeast
      GCN5 protein implicates the cleft and the N- and C-terminal protein segments as
      playing an important role in histone substrate binding, and a glutamate residue
      in the protein core as playing an essential catalytic role. A structural
      comparison with the coenzyme-bound forms of the related N-acetyltransferases,
      HAT1 (yeast histone acetyltransferase 1) and SmAAT (Serratia marcescens
      aminoglycoside 3-N-acetyltransferase), suggests the mode of substrate binding and
      catalysis by these enzymes and establishes a paradigm for understanding the
      structure-function relationships of other enzymes that acetylate histones and
      transcriptional regulators to promote activated transcription.
FAU - Clements, A
AU  - Clements A
AD  - The Wistar Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.
FAU - Rojas, J R
AU  - Rojas JR
FAU - Trievel, R C
AU  - Trievel RC
FAU - Wang, L
AU  - Wang L
FAU - Berger, S L
AU  - Berger SL
FAU - Marmorstein, R
AU  - Marmorstein R
LA  - eng
SI  - PDB/1CM0
GR  - GM52880/GM/NIGMS NIH HHS/United States
GR  - GM55360/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (Histones)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Transcription Factors)
RN  - 3KX376GY7L (Glutamic Acid)
RN  - EC 2.3.1.- (Acetyltransferases)
RN  - EC 2.3.1.48 (GCN5 protein, S cerevisiae)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
RN  - EC 2.7.- (Protein Kinases)
RN  - SAA04E81UX (Coenzyme A)
SB  - IM
MH  - Acetylation
MH  - Acetyltransferases/*chemistry/metabolism
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Catalysis
MH  - Coenzyme A/chemistry/*metabolism
MH  - Conserved Sequence
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - *DNA-Binding Proteins
MH  - Fungal Proteins/chemistry/metabolism
MH  - Glutamic Acid/chemistry/metabolism
MH  - Histone Acetyltransferases
MH  - Histones/metabolism
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Protein Kinases/chemistry/metabolism
MH  - Protein Structure, Secondary
MH  - *Saccharomyces cerevisiae Proteins
MH  - Structure-Activity Relationship
MH  - Transcription Factors/*chemistry/metabolism
PMC - PMC1171431
EDAT- 1999/07/07 00:00
MHDA- 1999/07/07 00:01
CRDT- 1999/07/07 00:00
PHST- 1999/07/07 00:00 [pubmed]
PHST- 1999/07/07 00:01 [medline]
PHST- 1999/07/07 00:00 [entrez]
AID - 10.1093/emboj/18.13.3521 [doi]
PST - ppublish
SO  - EMBO J. 1999 Jul 1;18(13):3521-32. doi: 10.1093/emboj/18.13.3521.