2c35

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|SITE=
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|ACTIVITY= [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]
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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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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c35 OCA], [http://www.ebi.ac.uk/pdbsum/2c35 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c35 RCSB]</span>
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[[Category: transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:37 2008''

Revision as of 23:15, 30 March 2008


PDB ID 2c35

Drag the structure with the mouse to rotate
, resolution 2.7Å
Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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