1a62
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1a62.gif|left|200px]] | [[Image:1a62.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1a62", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_1a62| PDB=1a62 | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO''' | '''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO''' | ||
Line 31: | Line 28: | ||
[[Category: Rule, G S.]] | [[Category: Rule, G S.]] | ||
[[Category: Wood, T C.]] | [[Category: Wood, T C.]] | ||
- | [[Category: | + | [[Category: F1-atpase]] |
- | [[Category: | + | [[Category: Ob fold]] |
- | [[Category: | + | [[Category: Rna binding domain]] |
- | [[Category: | + | [[Category: Termination]] |
- | [[Category: | + | [[Category: Transcription regulation]] |
- | [[Category: | + | [[Category: Transcription termination]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:51:52 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 06:51, 2 May 2008
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 Page seeded by OCA on Fri May 2 09:51:52 2008