1XQH: Crystal Structure Of A Ternary Complex Of The Methyltransferase Set9 (Also Known As Set79) WITH A P53 Peptide And Sah

Citation:
Abstract
p53 is a tumour suppressor that regulates the cellular response to genotoxic stresses. p53 is a short-lived protein and its activity is regulated mostly by stabilization via different post-translational modifications. Here we report a novel mechanism of p53 regulation through lysine methylation by Set9 methyltransferase. Set9 specifically methylates p53 at one residue within the carboxyl-terminus regulatory region. Methylated p53 is restricted to the nucleus and the modification positively affects its stability. Set9 regulates the expression of p53 target genes in a manner dependent on the p53-methylation site. The crystal structure of a ternary complex of Set9 with a p53 peptide and the cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular basis for recognition of p53 by this lysine methyltransferase.
PDB ID: 1XQHDownload
MMDB ID: 30734
PDB Deposition Date: 2004/10/12
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.75  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 1XQH: dimeric; determined by author and by software (PISA)
Molecular Components in 1XQH
Label Count Molecule
Proteins (2 molecules)
1
Histone-lysine N-methyltransferase, H3 Lysine-4 Specific(Gene symbol: SETD7)
Molecule annotation
1
9-mer Peptide From Tumor Protein P53(Gene symbol: TP53)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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