2c5z
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(New page: 200px<br /><applet load="2c5z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c5z" /> '''STRUCTURE AND CTD BINDING OF THE SET2 SRI DO...)
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Revision as of 06:54, 21 November 2007
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STRUCTURE AND CTD BINDING OF THE SET2 SRI DOMAIN
Overview
During mRNA elongation, the SRI domain of the histone H3 methyltransferase, Set2 binds to the phosphorylated carboxyl-terminal domain (CTD) of RNA, polymerase II. The solution structure of the yeast Set2 SRI domain reveals, a novel CTD-binding fold consisting of a left-handed three-helix bundle., NMR titration shows that the SRI domain binds an Ser2/Ser5-phosphorylated, CTD peptide comprising two heptapeptide repeats and three flanking, NH2-terminal residues, whereas a single CTD repeat is insufficient for, binding. Residues that show strong chemical shift perturbations upon CTD, binding cluster in two regions. Both CTD tyrosine side chains contact the, SRI domain. One of the tyrosines binds in the region with the strongest, chemical shift perturbations, formed by the two NH2-terminal helices., Unexpectedly, the SRI domain fold resembles the structure of an RNA, polymerase-interacting domain in bacterial sigma factors (domain sigma2 in, sigma70).
About this Structure
2C5Z is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription., Vojnic E, Simon B, Strahl BD, Sattler M, Cramer P, J Biol Chem. 2006 Jan 6;281(1):13-5. Epub 2005 Nov 14. PMID:16286474
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