2c35: Difference between revisions

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[[Image:2c35.gif|left|200px]]
[[Image:2c35.gif|left|200px]]


{{Structure
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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'''SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II'''
'''SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II'''
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[[Category: Onesti, S.]]
[[Category: Onesti, S.]]
[[Category: Werner, F.]]
[[Category: Werner, F.]]
[[Category: nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
[[Category: polymerase]]
[[Category: Polymerase]]
[[Category: rna polymerase ii]]
[[Category: Rna polymerase ii]]
[[Category: transcription]]
[[Category: Transcription]]
 
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Revision as of 21:10, 3 May 2008

File:2c35.gif

Template:STRUCTURE 2c35

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. 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 Page seeded by OCA on Sat May 3 21:10:42 2008

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