2c5z
From Proteopedia
(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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| - | [[Image:2c5z.gif|left|200px]]<br /><applet load="2c5z" size=" | + | [[Image:2c5z.gif|left|200px]]<br /><applet load="2c5z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2c5z" /> | caption="2c5z" /> | ||
'''STRUCTURE AND CTD BINDING OF THE SET2 SRI DOMAIN'''<br /> | '''STRUCTURE AND CTD BINDING OF THE SET2 SRI DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | During mRNA elongation, the SRI domain of the histone H3 methyltransferase | + | 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== | ==About this Structure== | ||
| - | 2C5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 2C5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sattler, M.]] | [[Category: Sattler, M.]] | ||
[[Category: Simon, B.]] | [[Category: Simon, B.]] | ||
| - | [[Category: Strahl, B | + | [[Category: Strahl, B D.]] |
[[Category: Vojnic, E.]] | [[Category: Vojnic, E.]] | ||
[[Category: ctd]] | [[Category: ctd]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:17 2008'' |
Revision as of 14:45, 21 February 2008
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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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