PDBsum entry 6duq

Transcription/RNA

PDB id: 6duq

Contents

Protein chains

(+ 6 more) 409 a.a.

(+ 6 more) 43 a.a.

DNA/RNA

Ligands

ADP ×12

BEF ×12

Metals

_MG ×12

PDB id:

6duq

Name:

Transcription/RNA

Title:

Structure of a rho-nusg kow domain complex

Structure:

Transcription termination factor rho. Chain: l, a, g, b, h, c, i, d, k, f, j, e. Synonym: atp-dependent helicase rho. Engineered: yes. Transcription termination/antitermination protein nusg. Chain: m, n, o, p, q, r, s, t, u, v, w, x. Engineered: yes. Ru12. Chain: y, z.

Source:

Escherichia coli m718. Organism_taxid: 656419. Gene: rho, ecjg_05123. Expressed in: escherichia coli. Expression_system_taxid: 562. Escherichia coli m605. Organism_taxid: 656417. Gene: nusg, ecig_05396. Synthetic: yes.

Resolution:

3.70Å R-factor: 0.288 R-free: 0.300

Authors:

J.M.Berger,M.R.Lawson

Key ref:

M.R.Lawson et al. (2018). Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein. Mol Cell, 71, 911. PubMed id: 30122535

Date:

21-Jun-18 Release date: 05-Sep-18

Protein chains

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

Seq: 419 a.a.

Struc: 409 a.a.

Protein chains

P0AFG0  (NUSG_ECOLI) -  Transcription termination/antitermination protein NusG from Escherichia coli (strain K12)

Seq: 181 a.a.

Struc: 43 a.a.

DNA/RNA chains

U-U-U-U-U-U 6 bases

U-U-U-U-U-U 6 bases

Enzyme reactions

• Enzyme class 2: Chains L, A, G, B, H, C, I, D, K, F, J, E: E.C.3.6.4.- - ?????
• Enzyme class 3: Chains M, N, O, P, Q, R, S, T, U, V, W, X: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Mol Cell 71:911 (2018)

PubMed id: 30122535

Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein.

M.R.Lawson, W.Ma, M.J.Bellecourt, I.Artsimovitch, A.Martin, R.Landick, K.Schulten, J.M.Berger.

ABSTRACT

NusG/Spt5 proteins are the only transcription factors utilized by all cellular organisms. In enterobacteria, NusG antagonizes the transcription termination activity of Rho, a hexameric helicase, during the synthesis of ribosomal and actively translated mRNAs. Paradoxically, NusG helps Rho act on untranslated transcripts, including non-canonical antisense RNAs and those arising from translational stress; how NusG fulfills these disparate functions is unknown. Here, we demonstrate that NusG activates Rho by assisting helicase isomerization from an open-ring, RNA-loading state to a closed-ring, catalytically active translocase. A crystal structure of closed-ring Rho in complex with NusG reveals the physical basis for this activation and further explains how Rho is excluded from translationally competent RNAs. This study demonstrates how a universally conserved transcription factor acts to modulate the activity of a ring-shaped ATPase motor and establishes how the innate sequence bias of a termination factor can be modulated to silence pervasive, aberrant transcription.