2LTO

TDRD3 complex

Summary for 2LTO

• Entry DOI: 10.2210/pdb2lto/pdb
• NMR Information: BMRB: 18490
• Descriptor: Tudor domain-containing protein 3, DNA-directed RNA polymerase II subunit RPB1 (2 entities in total)
• Functional Keywords: adma, transcription-transferase complex, transcription/transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q9H7E2; Nucleus : P24928
• Total number of polymer chains: 2
• Total formula weight: 8322.41

Authors

Sikorsky, T. (deposition date: 2012-05-30, release date: 2013-01-16, Last modification date: 2023-11-15)

Primary citation

Sikorsky, T.,Hobor, F.,Krizanova, E.,Pasulka, J.,Kubicek, K.,Stefl, R.
Recognition of asymmetrically dimethylated arginine by TDRD3.
Nucleic Acids Res., 40:11748-11755, 2012

PubMed Abstract: Asymmetric dimethylarginine (aDMA) marks are placed on histones and the C-terminal domain (CTD) of RNA Polymerase II (RNAP II) and serve as a signal for recruitment of appropriate transcription and processing factors in coordination with transcription cycle. In contrast to other Tudor domain-containing proteins, Tudor domain-containing protein 3 (TDRD3) associates selectively with the aDMA marks but not with other methylarginine motifs. Here, we report the solution structure of the Tudor domain of TDRD3 bound to the asymmetrically dimethylated CTD. The structure and mutational analysis provide a molecular basis for how TDRD3 recognizes the aDMA mark. The unique aromatic cavity of the TDRD3 Tudor domain with a tyrosine in position 566 creates a selectivity filter for the aDMA residue. Our work contributes to the understanding of substrate selectivity rules of the Tudor aromatic cavity, which is an important structural motif for reading of methylation marks.

PubMed: 23066109
DOI: 10.1093/nar/gks929

Experimental method

SOLUTION NMR