This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2c35
From Proteopedia
(New page: 200px<br /> <applet load="2c35" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c35, resolution 2.7Å" /> '''SUBUNITS RPB4 AND RP...) |
|||
| Line 1: | Line 1: | ||
| - | [[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" |
| - | <applet load="2c35" size=" | + | |
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== | ||
| Line 16: | Line 15: | ||
[[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.]] | ||
| Line 25: | Line 24: | ||
[[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 14:44, 21 February 2008
|
SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II
Overview
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
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.
Reference
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
Page seeded by OCA on Thu Feb 21 16:44:29 2008
