1sza

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(New page: 200px<br /><applet load="1sza" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sza, resolution 2.20&Aring;" /> '''The RNA polymerase I...)
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[[Image:1sza.gif|left|200px]]<br /><applet load="1sza" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sza, resolution 2.20&Aring;" />
caption="1sza, resolution 2.20&Aring;" />
'''The RNA polymerase II CTD in mRNA processing: beta-turn recognition and beta-spiral model'''<br />
'''The RNA polymerase II CTD in mRNA processing: beta-turn recognition and beta-spiral model'''<br />
==Overview==
==Overview==
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During transcription, RNA polymerase (Pol) II synthesizes eukaryotic, messenger RNA. Transcription is coupled to RNA processing by the, carboxy-terminal domain (CTD) of Pol II, which consists of up to 52, repeats of the sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 (refs 1, 2). After phosphorylation, the CTD binds tightly to a conserved, CTD-interacting domain (CID) present in the proteins Pcf11 and Nrd1, which, are essential and evolutionarily conserved factors for, polyadenylation-dependent and -independent 3'-RNA processing, respectively. Here we describe the structure of a Ser 2-phosphorylated CTD, peptide bound to the CID domain of Pcf11. The CTD motif Ser 2-Pro 3-Thr, 4-Ser 5 forms a beta-turn that binds to a conserved groove in the CID, domain. The Ser 2 phosphate group does not make direct contact with the, CID domain, but may be recognized indirectly because it stabilizes the, beta-turn with an additional hydrogen bond. Iteration of the peptide, structure results in a compact beta-spiral model of the CTD. The model, suggests that, during the mRNA transcription-processing cycle, compact, spiral regions in the CTD are unravelled and regenerated in a, phosphorylation-dependent manner.
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During transcription, RNA polymerase (Pol) II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing by the carboxy-terminal domain (CTD) of Pol II, which consists of up to 52 repeats of the sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 (refs 1, 2). After phosphorylation, the CTD binds tightly to a conserved CTD-interacting domain (CID) present in the proteins Pcf11 and Nrd1, which are essential and evolutionarily conserved factors for polyadenylation-dependent and -independent 3'-RNA processing, respectively. Here we describe the structure of a Ser 2-phosphorylated CTD peptide bound to the CID domain of Pcf11. The CTD motif Ser 2-Pro 3-Thr 4-Ser 5 forms a beta-turn that binds to a conserved groove in the CID domain. The Ser 2 phosphate group does not make direct contact with the CID domain, but may be recognized indirectly because it stabilizes the beta-turn with an additional hydrogen bond. Iteration of the peptide structure results in a compact beta-spiral model of the CTD. The model suggests that, during the mRNA transcription-processing cycle, compact spiral regions in the CTD are unravelled and regenerated in a phosphorylation-dependent manner.
==About this Structure==
==About this Structure==
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1SZA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SZA OCA].
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1SZA 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=1SZA OCA].
==Reference==
==Reference==
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[[Category: rna polymerase ii ctd interacting domain]]
[[Category: rna polymerase ii ctd interacting domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:51:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:40 2008''

Revision as of 13:07, 21 February 2008


1sza, resolution 2.20Å

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The RNA polymerase II CTD in mRNA processing: beta-turn recognition and beta-spiral model

Overview

During transcription, RNA polymerase (Pol) II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing by the carboxy-terminal domain (CTD) of Pol II, which consists of up to 52 repeats of the sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 (refs 1, 2). After phosphorylation, the CTD binds tightly to a conserved CTD-interacting domain (CID) present in the proteins Pcf11 and Nrd1, which are essential and evolutionarily conserved factors for polyadenylation-dependent and -independent 3'-RNA processing, respectively. Here we describe the structure of a Ser 2-phosphorylated CTD peptide bound to the CID domain of Pcf11. The CTD motif Ser 2-Pro 3-Thr 4-Ser 5 forms a beta-turn that binds to a conserved groove in the CID domain. The Ser 2 phosphate group does not make direct contact with the CID domain, but may be recognized indirectly because it stabilizes the beta-turn with an additional hydrogen bond. Iteration of the peptide structure results in a compact beta-spiral model of the CTD. The model suggests that, during the mRNA transcription-processing cycle, compact spiral regions in the CTD are unravelled and regenerated in a phosphorylation-dependent manner.

About this Structure

1SZA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors., Meinhart A, Cramer P, Nature. 2004 Jul 8;430(6996):223-6. PMID:15241417

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