2c35: Difference between revisions
New page: left|200px<br /> <applet load="2c35" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c35, resolution 2.7Å" /> '''SUBUNITS RPB4 AND RP... |
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[[Image:2c35.gif|left|200px]]<br /> | [[Image:2c35.gif|left|200px]]<br /><applet load="2c35" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2c35, resolution 2.7Å" /> | caption="2c35, resolution 2.7Å" /> | ||
'''SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II'''<br /> | '''SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II'''<br /> | ||
==Overview== | ==Overview== | ||
The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAP(II)) form | The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAP(II)) form a heterodimer that protrudes from the 10-subunit core of the enzyme. We have obtained crystals of the human Rpb4/Rpb7 heterodimer and determined the structure to 2.7 A resolution. The presence of putative RNA-binding domains on the Rpb7 subunit and the position of the heterodimer close to the RNA exit groove in the 12 subunit yeast polymerase complex strongly suggests a role for the heterodimer in binding and stabilizing the nascent RNA transcript. We have complemented the structural analysis with biochemical studies directed at dissecting the RNA-binding properties of the human Rpb4/Rpb7 complex and that of the homologous E/F complex from Methanocaldococcus jannaschii. A number of conserved, solvent-exposed residues in both the human Rpb7 subunit and the archaeal E subunit have been modified by site-directed mutagenesis and the mutants tested for RNA binding by performing electrophoretic mobility shift assays. These studies have identified an elongated surface region on the corresponding face of both subunit E and Rpb7 that is involved in RNA binding. The area spans the nucleic acid binding face of the OB fold, including the B4-B5 loop, but also extends towards the N-terminal domain. | ||
==About this Structure== | ==About this Structure== | ||
2C35 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http:// | 2C35 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C35 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Brick, P.]] | [[Category: Brick, P.]] | ||
[[Category: Cordell, S | [[Category: Cordell, S C.]] | ||
[[Category: Meka, H.]] | [[Category: Meka, H.]] | ||
[[Category: Onesti, S.]] | [[Category: Onesti, S.]] | ||
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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 16:44:29 2008'' | ||
Revision as of 17:44, 21 February 2008
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SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II
OverviewOverview
The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAP(II)) form a heterodimer that protrudes from the 10-subunit core of the enzyme. We have obtained crystals of the human Rpb4/Rpb7 heterodimer and determined the structure to 2.7 A resolution. The presence of putative RNA-binding domains on the Rpb7 subunit and the position of the heterodimer close to the RNA exit groove in the 12 subunit yeast polymerase complex strongly suggests a role for the heterodimer in binding and stabilizing the nascent RNA transcript. We have complemented the structural analysis with biochemical studies directed at dissecting the RNA-binding properties of the human Rpb4/Rpb7 complex and that of the homologous E/F complex from Methanocaldococcus jannaschii. A number of conserved, solvent-exposed residues in both the human Rpb7 subunit and the archaeal E subunit have been modified by site-directed mutagenesis and the mutants tested for RNA binding by performing electrophoretic mobility shift assays. These studies have identified an elongated surface region on the corresponding face of both subunit E and Rpb7 that is involved in RNA binding. The area spans the nucleic acid binding face of the OB fold, including the B4-B5 loop, but also extends towards the N-terminal domain.
About this StructureAbout this Structure
2C35 is a Protein complex structure of sequences from Homo sapiens. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA polymerase II., Meka H, Werner F, Cordell SC, Onesti S, Brick P, Nucleic Acids Res. 2005 Nov 10;33(19):6435-44. Print 2005. PMID:16282592
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