3QQC

Crystal structure of archaeal Spt4/5 bound to the RNAP clamp domain

Summary for 3QQC

• Entry DOI: 10.2210/pdb3qqc/pdb
• Descriptor: DNA-directed RNA polymerase subunit b, DNA-directed RNA polymerase subunit a', DNA-directed RNA polymerase subunit A'', Transcription antitermination protein nusG, DNA-directed RNA polymerase, subunit e'', ... (4 entities in total)
• Functional Keywords: transcription, fusion protein, chimera protein, multiprotein complex
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 3
• Total formula weight: 74737.54

Authors

Martinez-Rucobo, F.W. (deposition date: 2011-02-15, release date: 2011-03-23, Last modification date: 2023-09-13)

Primary citation

Martinez-Rucobo, F.W.,Sainsbury, S.,Cheung, A.C.,Cramer, P.
Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity.
Embo J., 30:1302-1310, 2011

PubMed Abstract: Related RNA polymerases (RNAPs) carry out cellular gene transcription in all three kingdoms of life. The universal conservation of the transcription machinery extends to a single RNAP-associated factor, Spt5 (or NusG in bacteria), which renders RNAP processive and may have arisen early to permit evolution of long genes. Spt5 associates with Spt4 to form the Spt4/5 heterodimer. Here, we present the crystal structure of archaeal Spt4/5 bound to the RNAP clamp domain, which forms one side of the RNAP active centre cleft. The structure revealed a conserved Spt5-RNAP interface and enabled modelling of complexes of Spt4/5 counterparts with RNAPs from all kingdoms of life, and of the complete yeast RNAP II elongation complex with bound Spt4/5. The N-terminal NGN domain of Spt5/NusG closes the RNAP active centre cleft to lock nucleic acids and render the elongation complex stable and processive. The C-terminal KOW1 domain is mobile, but its location is restricted to a region between the RNAP clamp and wall above the RNA exit tunnel, where it may interact with RNA and/or other factors.

PubMed: 21386817
DOI: 10.1038/emboj.2011.64

Experimental method

X-RAY DIFFRACTION (3.3 Å)