8H2N

gp96 RNA polymerase from P23-45 phage (crystal 2)

8H2N の概要

• エントリーDOI: 10.2210/pdb8h2n/pdb
• 分子名称: Tape tail measure protein, MAGNESIUM ION (2 entities in total)
• 機能のキーワード: rna polymerase, transcription
• 由来する生物種: Thermus virus P23-45 (Thermus thermophilus phage P23-45)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 368289.47

構造登録者

Chaban, A.,Sokolova, M.L.,Tagami, S. (登録日: 2022-10-06, 公開日: 2023-10-11, 最終更新日: 2024-11-13)

主引用文献

Chaban, A.,Minakhin, L.,Goldobina, E.,Bae, B.,Hao, Y.,Borukhov, S.,Putzeys, L.,Boon, M.,Kabinger, F.,Lavigne, R.,Makarova, K.S.,Koonin, E.V.,Nair, S.K.,Tagami, S.,Severinov, K.,Sokolova, M.L.
Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail.
Nat Commun, 15:317-317, 2024

PubMed Abstract: Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species.

PubMed: 38182597
DOI: 10.1038/s41467-023-44630-z

実験手法

X-RAY DIFFRACTION (4.41 Å)