4O30: Crystal Structure Of Atxr5 In Complex With Histone H3.1 And Adohcy

Citation:
Abstract
Histone variants have been proposed to act as determinants for posttranslational modifications with widespread regulatory functions. We identify a histone-modifying enzyme that selectively methylates the replication-dependent histone H3 variant H3.1. The crystal structure of the SET domain of the histone H3 lysine-27 (H3K27) methyltransferase ARABIDOPSIS TRITHORAX-RELATED PROTEIN 5 (ATXR5) in complex with a H3.1 peptide shows that ATXR5 contains a bipartite catalytic domain that specifically "reads" alanine-31 of H3.1. Variation at position 31 between H3.1 and replication-independent H3.3 is conserved in plants and animals, and threonine-31 in H3.3 is responsible for inhibiting the activity of ATXR5 and its paralog, ATXR6. Our results suggest a simple model for the mitotic inheritance of the heterochromatic mark H3K27me1 and the protection of H3.3-enriched genes against heterochromatization during DNA replication.
PDB ID: 4O30Download
MMDB ID: 118657
PDB Deposition Date: 2013/12/17
Updated in MMDB: 2014/10
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 4O30: dimeric; determined by author and by software (PISA)
Molecular Components in 4O30
Label Count Molecule
Proteins (2 molecules)
1
Histone-lysine N-methyltransferase Atxr6, Putative(Gene symbol: LOC8259125)
Molecule annotation
1
Histone H3.1
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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