5BKH
The splicing activity and an alternative domain-swapped structure of the Pyrococcus horikoshii PolII mini-intein
Summary for 5BKH
| Entry DOI | 10.2210/pdb5bkh/pdb |
| Descriptor | DNA polymerase II large subunit (2 entities in total) |
| Functional Keywords | intein, hydrolase |
| Biological source | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Total number of polymer chains | 1 |
| Total formula weight | 21679.65 |
| Authors | |
| Primary citation | 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 Cited by 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: 34083592DOI: 10.1038/s41598-021-91090-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
Download full validation report
