1utu
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(New page: 200px<br /> <applet load="1utu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1utu, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 17:32, 12 November 2007
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CRYSTAL STRUCTURE OF NOVEL PROTEIN EMSY TRUNCATE
Overview
EMSY is a large nuclear protein that binds to the transactivation domain, of BRCA2. EMSY contains an approximately 100-residue segment at the amino, terminus called the ENT (EMSY N-terminal) domain. Plant proteins, containing ENT domains also contain members of the royal family of, chromatin-remodelling domains. It has been proposed that EMSY may have a, role in chromatin-related processes. This is supported by the observation, that a number of chromatin-regulator proteins, including HP1beta and BS69, bind directly to EMSY by means of a conserved motif adjacent to the ENT, domain. Here, we report the crystal structure of residues 1-108 of EMSY at, 2.0 A resolution. The structure contains both the ENT domain and the, HP1beta/BS69-binding motif. This binding motif forms an extended, peptide-like conformation that adopts distinct orientations in each, subunit of the dimer. Biophysical and nuclear magnetic resonance analyses, show that the main complex formed by EMSY and the chromoshadow domain of, HP1 (HP1-CSD) consists of one EMSY dimer sandwiched between two HP1-CSD, dimers. The HP1beta-binding motif is necessary and sufficient for EMSY to, bind to the chromoshadow domain of HP1beta.
About this Structure
1UTU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69., Ekblad CM, Chavali GB, Basu BP, Freund SM, Veprintsev D, Hughes-Davies L, Kouzarides T, Doherty AJ, Itzhaki LS, EMBO Rep. 2005 Jul;6(7):675-80. PMID:15947784
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