3LPE

Crystal structure of Spt4/5NGN heterodimer complex from Methanococcus jannaschii

Summary for 3LPE

• Entry DOI: 10.2210/pdb3lpe/pdb
• Related: 1RYQ 3EWG
• Descriptor: Putative transcription antitermination protein nusG, DNA-directed RNA polymerase subunit E'', ZINC ION, ... (4 entities in total)
• Functional Keywords: transcription regulation, spt4, spt5, nusg, archaea, evolution, dna-directed rna polymerase, metal-binding, nucleotidyltransferase, transcription, transferase, zinc-finger
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii); More
• Total number of polymer chains: 8
• Total formula weight: 66354.97

Authors

Hirtreiter, A.,Damsma, G.E.,Cheung, A.C.M.,Klose, D.,Grohmann, D.,Vojnic, E.,Martin, A.C.R.,Cramer, P.,Werner, F. (deposition date: 2010-02-05, release date: 2010-03-09, Last modification date: 2023-11-01)

Primary citation

Hirtreiter, A.,Damsma, G.E.,Cheung, A.C.,Klose, D.,Grohmann, D.,Vojnic, E.,Martin, A.C.,Cramer, P.,Werner, F.
Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif.
Nucleic Acids Res., 38:4040-4051, 2010

PubMed Abstract: Spt5 is the only known RNA polymerase-associated factor that is conserved in all three domains of life. We have solved the structure of the Methanococcus jannaschii Spt4/5 complex by X-ray crystallography, and characterized its function and interaction with the archaeal RNAP in a wholly recombinant in vitro transcription system. Archaeal Spt4 and Spt5 form a stable complex that associates with RNAP independently of the DNA-RNA scaffold of the elongation complex. The association of Spt4/5 with RNAP results in a stimulation of transcription processivity, both in the absence and the presence of the non-template strand. A domain deletion analysis reveals the molecular anatomy of Spt4/5--the Spt5 Nus-G N-terminal (NGN) domain is the effector domain of the complex that both mediates the interaction with RNAP and is essential for its elongation activity. Using a mutagenesis approach, we have identified a hydrophobic pocket on the Spt5 NGN domain as binding site for RNAP, and reciprocally the RNAP clamp coiled-coil motif as binding site for Spt4/5.

PubMed: 20197319
DOI: 10.1093/nar/gkq135

Experimental method

X-RAY DIFFRACTION (1.9 Å)