1pvo

From Proteopedia

Revision as of 09:50, 11 March 2013

spinqualitylabelsall models PDB ID 1pvo Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1pvo, resolution 3.00Å ()
Ligands:
Gene:	RHO (Escherichia coli)
Related:	1pv4
Structural annotation: Resources: InterPro : Ipr011112, Ipr011129, Ipr002110, Ipr000194, Ipr004665, Ipr003593, Ipr011113 Pfam : PF07498, PF00006, PF07497 SCOP : d1pvoa2, d1pvoa3, d1pvoa1, d1pvob1, d1pvob2, d1pvoc3, d1pvoc2, d1pvoc1, d1pvod2, d1pvod1, d1pvod3, d1pvoe3, d1pvoe2, d1pvoe1, d1pvof1, d1pvof3, d1pvof2 UniProt : P0AG30
Functional annotation: Cellular component: proton-transporting two-sector ATPase complex membrane fraction Biological process: transcription termination transcription regulation of transcription, DNA-dependent ATP synthesis coupled proton transport Molecular function: protein binding hydrogen ion transporting ATP synthase activity, rotational mechanism hydrogen ion transporting ATPase activity, rotational mechanism nucleotide binding helicase activity transcription termination factor activity RNA binding ATP binding nucleoside-triphosphatase activity hydrolase activity nucleic acid binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP

Template:ABSTRACT PUBMED 12859904

About this Structure

1pvo is a 11 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

• Helicase
• Transcription Termination Factor Rho

Reference

• Skordalakes E, Berger JM. Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading. Cell. 2003 Jul 11;114(1):135-46. PMID:12859904