spacer
View the latest EBI news stories and important announcements...
more

spacer
Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1bob

E.C. namehistone acetyltransferase
SpeciesSaccharomyces cerevisiae (Baker's yeast)
E.C. Number (IntEnz) 2.3.1.48
CSA Homologues of 1bob
CSA Entries With UniProtID Q12341
CSA Entries With EC Number 2.3.1.48
PDBe Entry 1bob
PDBSum Entry 1bob
MACiE Entry M0224

Literature Report

IntroductionHat1, isolated from Saccharomyces cerevisiae, is a type B histone acetyltransferase. It catalyses the sequential acetylation of Lys12 and then Lys5 of newly synthesised histone H4 using acetyl-CoA as the source of the acetyl group. Hat1 associates with the accessory protein Hat2 before binding and acetylating H4. The complex is thought to also bind histone H3. The complex is then imported into the nucleus where the histones are deposited onto DNA with the aid of Hif1. Hat1 is unable to acetylate DNA-associated histones.
MechansimGlu255 deprotonates Lys12 of H4 and the neutral amine is the nucleophile for attack on the carbonyl of acetyl-CoA. The resulting tetrahedral intermediate collapses back and eliminates CoAS-, which is protonated by an as yet unknown acid. The process is then repeated with Lys5 of H4.
Reaction

Catalytic Sites for 1bob

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA255255macie:sideChainGlu255 removes a proton from Lys12/Lys5 of H4 to produce the neutral amine, which is a better nucleophile for attack on acetyl CoA.

Literature References

Notes:
Poveda A
Site specificity of yeast histone acetyltransferase B complex in vivo.
FEBS J 2008 275 2122-2136
PubMed: 18373695
Parthun MR.
Hat1: the emerging cellular roles of a type B histone acetyltransferase.
Oncogene 2007 26 5319-5328
PubMed: 17694075
Trievel RC
Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.
Proc Natl Acad Sci U S A 1999 96 8931-8936
PubMed: 10430873
Dutnall RN
Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.
Cell 1998 94 427-438
PubMed: 9727486
spacer
spacer