PDBsum entry 3io2

Transferase

PDB id: 3io2

Contents

Protein chain

109 a.a. *

Ligands

SO4 ×4

Metals

_ZN ×3

Waters ×31

* Residue conservation analysis

PDB id:

3io2

Name:

Transferase

Title:

Crystal structure of the taz2 domain of p300

Structure:

Histone acetyltransferase p300. Chain: a. Fragment: residues 1723-1836. Synonym: p300 hat, e1a-associated protein p300. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ep300, p300. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.50Å R-factor: 0.208 R-free: 0.236

Authors:

M.Miller,Z.Dauter,A.Wlodawer

Key ref:

M.Miller et al. (2009). Structure of the Taz2 domain of p300: insights into ligand binding. Acta Crystallogr D Biol Crystallogr, 65, 1301-1308. PubMed id: 19966416

Date:

13-Aug-09 Release date: 24-Nov-09

Protein chain

Q09472  (EP300_HUMAN) -  Histone acetyltransferase p300 from Homo sapiens

Seq: 2414 a.a.

Struc: 109 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: E.C.2.3.1.- - ?????
• Enzyme class 2: E.C.2.3.1.48 - histone acetyltransferase.
• Reaction: L-lysyl-[protein] + acetyl-CoA = N₆-acetyl-L-lysyl-[protein] + CoA + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

Acta Crystallogr D Biol Crystallogr 65:1301-1308 (2009)

PubMed id: 19966416

Structure of the Taz2 domain of p300: insights into ligand binding.

M.Miller, Z.Dauter, S.Cherry, J.E.Tropea, A.Wlodawer.

ABSTRACT

CBP and its paralog p300 are histone acetyl transferases that regulate gene expression by interacting with multiple transcription factors via specialized domains. The structure of a segment of human p300 protein (residues 1723-1836) corresponding to the extended zinc-binding Taz2 domain has been investigated. The crystal structure was solved by the SAD approach utilizing the anomalous diffraction signal of the bound Zn ions. The structure comprises an atypical helical bundle stabilized by three Zn ions and closely resembles the solution structures determined previously for shorter peptides. Residues 1813-1834 from the current construct form a helical extension of the C-terminal helix and make extensive crystal-contact interactions with the peptide-binding site of Taz2, providing additional insights into the mechanism of the recognition of diverse transactivation domains (TADs) by Taz2. On the basis of these results and molecular modeling, a hypothetical model of the binding of phosphorylated p53 TAD1 to Taz2 has been proposed.