1A62

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

PDB DOI: https://doi.org/10.2210/pdb1A62/pdb

Classification: TRANSCRIPTION TERMINATION
Organism(s): Escherichia coli BL21(DE3)
Expression System: Escherichia coli BL21(DE3)
Mutation(s): Yes

Deposited: 1998-03-05 Released: 1998-06-17
Deposition Author(s): Allison, T.J., Wood, T.C., Briercheck, D.M., Rastinejad, F., Richardson, J.P., Rule, G.S.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.55 Å
R-Value Free: 0.250
R-Value Work: 0.216
R-Value Observed: 0.216

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Crystal structure of the RNA-binding domain from transcription termination factor rho.

Allison, T.J., Wood, T.C., Briercheck, D.M., Rastinejad, F., Richardson, J.P., Rule, G.S.

(1998) Nat Struct Biol 5: 352-356

PubMed: 9586995 Search on PubMed
DOI: https://doi.org/10.1038/nsb0598-352
Primary Citation of Related Structures:
1A62

PubMed Abstract:
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.

Macromolecule Content

Total Structure Weight: 14.78 kDa
Atom Count: 1,102
Modelled Residue Count: 125
Deposited Residue Count: 130
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
RHO	A	130	Escherichia coli BL21(DE3)	Mutation(s): 2
UniProt
Find proteins for P0AG30 (Escherichia coli (strain K12)) Explore P0AG30 Go to UniProtKB: P0AG30
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0AG30
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.55 Å
R-Value Free: 0.250
R-Value Work: 0.216
R-Value Observed: 0.216
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 25.95	α = 90
b = 56.01	β = 99.35
c = 42.92	γ = 90

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
DENZO	data reduction
SCALEPACK	data scaling
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1998-06-17

Deposition Author(s):

Briercheck, D.M.

Richardson, J.P.

Revision History (Full details and data files)

Version 1.0: 1998-06-17
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.