PDBsum entry 2ht1

Hydrolase/RNA

PDB id: 2ht1

Contents

Protein chains

324 a.a. *

DNA/RNA

Ligands

__U-__C ×2

SO4 ×2

* Residue conservation analysis

PDB id:

2ht1

Name:

Hydrolase/RNA

Title:

The closed ring structure of the rho transcription termination factor in complex with nucleic acid in the motor domains

Structure:

5'-r( Up C)-3'. Chain: j, k. Engineered: yes. 5'-r( Up Cp Up Cp U)-3'. Chain: m. Engineered: yes. Transcription termination factor rho. Chain: a, b. Synonym: atp-dependent helicase rho.

Source:

Synthetic: yes. Escherichia coli. Organism_taxid: 562. Gene: rho, nita, psua, rnsc, sbaa, tsu. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Monomer (from PDB file)

Resolution:

3.51Å R-factor: 0.287 R-free: 0.328

Authors:

E.Skordalakes,J.M.Berger

Key ref:

E.Skordalakes and J.M.Berger (2006). Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell, 127, 553-564. PubMed id: 17081977 DOI: 10.1016/j.cell.2006.08.051

Date:

24-Jul-06 Release date: 14-Nov-06

Protein chains

P0AG30  (RHO_ECOLI) -  Transcription termination factor Rho from Escherichia coli (strain K12)

Seq: 419 a.a.

Struc: 324 a.a.

DNA/RNA chain

U-C-U-C-U 5 bases

Enzyme reactions

• Enzyme class: E.C.3.6.4.- - ?????

DOI no: 10.1016/j.cell.2006.08.051

Cell 127:553-564 (2006)

PubMed id: 17081977

Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor.

E.Skordalakes, J.M.Berger.

ABSTRACT

Hexameric helicases and translocases are required for numerous essential nucleic-acid transactions. To better understand the mechanisms by which these enzymes recognize target substrates and use nucleotide hydrolysis to power molecular movement, we have determined the structure of the Rho transcription termination factor, a hexameric RNA/DNA helicase, with single-stranded RNA bound to the motor domains of the protein. The structure reveals a closed-ring "trimer of dimers" conformation for the hexamer that contains an unanticipated arrangement of conserved loops required for nucleic-acid translocation. RNA extends across a shallow intersubunit channel formed by conserved amino acids required for RNA-stimulated ATP hydrolysis and translocation and directly contacts a conserved lysine, just upstream of the catalytic GKT triad, in the phosphate-binding (P loop) motif of the ATP-binding pocket. The structure explains the molecular effects of numerous mutations and provides new insights into the links between substrate recognition, ATP turnover, and coordinated strand movement.

Selected figure(s)

Figure 1.
Figure 1. Rho Protomer Structure

Figure 3.
Figure 3. Primary and Secondary RNA-Binding Sites of Rho

The above figures are reprinted by permission from Cell Press: Cell (2006, 127, 553-564) copyright 2006.

Figures were selected by an automated process.