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1a62
From Proteopedia
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| - | [[Image:1a62.gif|left|200px]] | + | [[Image:1a62.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO''' | + | {{Structure |
| + | |PDB= 1a62 |SIZE=350|CAPTION= <scene name='initialview01'>1a62</scene>, resolution 1.55Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A62 is a [ | + | 1A62 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A62 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9586995 9586995] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription termination]] | [[Category: transcription termination]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:26 2008'' |
Revision as of 07:53, 20 March 2008
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| , resolution 1.55Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 09:53:26 2008
