3MTS

Chromo Domain of Human Histone-Lysine N-Methyltransferase SUV39H1

Summary for 3MTS

• Entry DOI: 10.2210/pdb3mts/pdb
• Descriptor: Histone-lysine N-methyltransferase SUV39H1 (2 entities in total)
• Functional Keywords: histone methyltransferase, histone-lysine n-methyltransferase, suv39h1, histone h3, tri-methylation, epigenetics, transcriptional repression, transcription regulation, chromatin, chromo domain, pre-set domain, set domain, post-set domain, structural genomics consortium, sgc, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O43463
• Total number of polymer chains: 3
• Total formula weight: 24300.78

Authors

Lam, R.,Li, Z.,Wang, J.,Crombet, L.,Walker, J.R.,Ouyang, H.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2010-04-30, release date: 2010-06-30, Last modification date: 2023-09-06)

Primary citation

Wang, T.,Xu, C.,Liu, Y.,Fan, K.,Li, Z.,Sun, X.,Ouyang, H.,Zhang, X.,Zhang, J.,Li, Y.,Mackenzie, F.,Min, J.,Tu, X.
Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3.
Plos One, 7:e52977-e52977, 2012

PubMed Abstract: SUV39H1, the first identified histone lysine methyltransferase in human, is involved in chromatin modification and gene regulation. SUV39H1 contains a chromodomain in its N-terminus, which potentially plays a role in methyl-lysine recognition and SUV39H1 targeting. In this study, the structure of the chromodomain of human SUV39H1 was determined by X-ray crystallography. The SUV39H1 chromodomain displays a generally conserved structure fold compared with other solved chromodomains. However, different from other chromodomains, the SUV39H1 chromodomain possesses a much longer helix at its C-terminus. Furthermore, the SUV39H1 chromodomain was shown to recognize histone H3K9me2/3 specifically.

PubMed: 23285239
DOI: 10.1371/journal.pone.0052977

Experimental method

X-RAY DIFFRACTION (2.2 Å)