3P8B

X-ray crystal structure of Pyrococcus furiosus transcription elongation factor Spt4/5

Summary for 3P8B

• Entry DOI: 10.2210/pdb3p8b/pdb
• Descriptor: DNA-directed RNA polymerase, subunit e'', Transcription antitermination protein nusG, ZINC ION, ... (6 entities in total)
• Functional Keywords: transcription elongation factor, rna polymerase, transferase-transcription complex, transferase/transcription
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 4
• Total formula weight: 52966.11

Authors

Murakami, K.S.,Klein, B.J. (deposition date: 2010-10-13, release date: 2011-01-26, Last modification date: 2024-02-21)

Primary citation

Klein, B.J.,Bose, D.,Baker, K.J.,Yusoff, Z.M.,Zhang, X.,Murakami, K.S.
RNA polymerase and transcription elongation factor Spt4/5 complex structure.
Proc.Natl.Acad.Sci.USA, 108:546-550, 2011

PubMed Abstract: Spt4/5 in archaea and eukaryote and its bacterial homolog NusG is the only elongation factor conserved in all three domains of life and plays many key roles in cotranscriptional regulation and in recruiting other factors to the elongating RNA polymerase. Here, we present the crystal structure of Spt4/5 as well as the structure of RNA polymerase-Spt4/5 complex using cryoelectron microscopy reconstruction and single particle analysis. The Spt4/5 binds in the middle of RNA polymerase claw and encloses the DNA, reminiscent of the DNA polymerase clamp and ring helicases. The transcription elongation complex model reveals that the Spt4/5 is an upstream DNA holder and contacts the nontemplate DNA in the transcription bubble. These structures reveal that the cellular RNA polymerases also use a strategy of encircling DNA to enhance its processivity as commonly observed for many nucleic acid processing enzymes including DNA polymerases and helicases.

PubMed: 21187417
DOI: 10.1073/pnas.1013828108

Experimental method

X-RAY DIFFRACTION (1.8 Å)