1a62

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|PDB= 1a62 |SIZE=350|CAPTION= <scene name='initialview01'>1a62</scene>, resolution 1.55&Aring;
|PDB= 1a62 |SIZE=350|CAPTION= <scene name='initialview01'>1a62</scene>, resolution 1.55&Aring;
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a62 OCA], [http://www.ebi.ac.uk/pdbsum/1a62 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a62 RCSB]</span>
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[[Category: transcription termination]]
[[Category: transcription termination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:07 2008''

Revision as of 15:34, 30 March 2008


PDB ID 1a62

Drag the structure with the mouse to rotate
, resolution 1.55Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO


Overview

Transcription termination factor rho is an ATP-dependent hexameric helicase found in most eubacterial species. The Escherichia coli rho monomer consists of two domains, an RNA-binding domain (residues 1-130) and an ATPase domain (residues 131-419). The ATPase domain is homologous to the beta subunit of F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms that rho130 contains the oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded beta-barrel. The beta-barrel of rho130 is also surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending the applicability of F1 ATPase as a structural model for hexameric rho.

About this Structure

1A62 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the RNA-binding domain from transcription termination factor rho., Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS, Nat Struct Biol. 1998 May;5(5):352-6. PMID:9586995

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