5BKH

The splicing activity and an alternative domain-swapped structure of the Pyrococcus horikoshii PolII mini-intein

5BKH の概要

• エントリーDOI: 10.2210/pdb5bkh/pdb
• 分子名称: DNA polymerase II large subunit (2 entities in total)
• 機能のキーワード: intein, hydrolase
• 由来する生物種: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21679.65

構造登録者

Li, Z.,Li, H. (登録日: 2021-03-19, 公開日: 2021-08-11, 最終更新日: 2024-05-22)

主引用文献

Williams, J.E.,Jaramillo, M.V.,Li, Z.,Zhao, J.,Wang, C.,Li, H.,Mills, K.V.
An alternative domain-swapped structure of the Pyrococcus horikoshii PolII mini-intein.
Sci Rep, 11:11680-11680, 2021

PubMed Abstract: Protein splicing is a post-translational process by which an intein catalyzes its own excision from flanking polypeptides, or exteins, concomitant with extein ligation. Many inteins have nested homing endonuclease domains that facilitate their propagation into intein-less alleles, whereas other inteins lack the homing endonuclease (HEN) and are called mini-inteins. The mini-intein that interrupts the DNA PolII of Pyrococcus horikoshii has a linker region in place of the HEN domain that is shorter than the linker in a closely related intein from Pyrococcus abyssi. The P. horikoshii PolII intein requires a higher temperature for catalytic activity and is more stable to digestion by the thermostable protease thermolysin, suggesting that it is more rigid than the P. abyssi intein. We solved a crystal structure of the intein precursor that revealed a domain-swapped dimer. Inteins found as domain swapped dimers have been shown to promote intein-mediated protein alternative splicing, but the solved P. horikoshii PolII intein structure has an active site unlikely to be catalytically competent.

PubMed: 34083592
DOI: 10.1038/s41598-021-91090-w

実験手法

X-RAY DIFFRACTION (2.43 Å)