7OGR

Structure of the apo-state of the bacteriophage PhiKZ non-virion RNA polymerase

Summary for 7OGR

• Entry DOI: 10.2210/pdb7ogr/pdb
• EMDB information: 12885 12886
• Descriptor: UNK helices, PHIKZ055, PHIKZ068, ... (7 entities in total)
• Functional Keywords: rna polymerase, phikz, non-virion, transcription
• Biological source: Pseudomonas phage phiKZ; More
• Total number of polymer chains: 6
• Total formula weight: 339456.16

Authors

de Martin Garrido, N.,Lai Wan Loong, Y.T.E.,Yakunina, M.,Aylett, C.H.S. (deposition date: 2021-05-07, release date: 2021-07-07, Last modification date: 2023-11-22)

Primary citation

deYMartin Garrido, N.,Orekhova, M.,Lai Wan Loong, Y.T.E.,Litvinova, A.,Ramlaul, K.,Artamonova, T.,Melnikov, A.S.,Serdobintsev, P.,Aylett, C.H.S.,Yakunina, M.
Structure of the bacteriophage PhiKZ non-virion RNA polymerase.
Nucleic Acids Res., 49:7732-7739, 2021

PubMed Abstract: Bacteriophage ΦKZ (PhiKZ) is the archetype of a family of massive bacterial viruses. It is considered to have therapeutic potential as its host, Pseudomonas aeruginosa, is an opportunistic, intrinsically antibiotic resistant, pathogen that kills tens of thousands worldwide each year. ΦKZ is an incredibly interesting virus, expressing many systems that the host already possesses. On infection, it forms a 'nucleus', erecting a barrier around its genome to exclude host endonucleases and CRISPR-Cas systems. ΦKZ infection is independent of the host transcriptional apparatus. It expresses two different multi-subunit RNA polymerases (RNAPs): the virion RNAP (vRNAP) is injected with the viral DNA during infection to transcribe early genes, including those encoding the non-virion RNAP (nvRNAP), which transcribes all further genes. ΦKZ nvRNAP is formed by four polypeptides thought to represent homologues of the eubacterial β/β' subunits, and a fifth with unclear homology, but essential for transcription. We have resolved the structure of ΦKZ nvRNAP to better than 3.0 Å, shedding light on its assembly, homology, and the biological role of the fifth subunit: it is an embedded, integral member of the complex, the position, structural homology and biochemical role of which imply that it has evolved from an ancestral homologue to σ-factor.

PubMed: 34181731
DOI: 10.1093/nar/gkab539

Experimental method

ELECTRON MICROSCOPY (3 Å)