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7QSS

Crystal structure of homing endonuclease-associated TliVMA intein (C1A)

Summary for 7QSS
Entry DOI10.2210/pdb7qss/pdb
DescriptorV-type ATP synthase alpha chain, FORMIC ACID (3 entities in total)
Functional Keywordsintein, protein splicing, endonuclease, hydrolase
Biological sourceThermococcus litoralis
Total number of polymer chains1
Total formula weight48982.42
Authors
Beyer, H.M.,Iwai, H. (deposition date: 2022-01-14, release date: 2022-03-30, Last modification date: 2024-01-31)
Primary citationBeyer, H.M.,Iwai, H.
Structural Basis for the Propagation of Homing Endonuclease-Associated Inteins.
Front Mol Biosci, 9:855511-855511, 2022
Cited by
PubMed Abstract: Inteins catalyze their removal from a host protein through protein splicing. Inteins that contain an additional site-specific endonuclease domain display genetic mobility via a process termed "homing" and thereby act as selfish DNA elements. We elucidated the crystal structures of two archaeal inteins associated with an active or inactive homing endonuclease domain. This analysis illustrated structural diversity in the accessory domains (ACDs) associated with the homing endonuclease domain. To augment homing endonucleases with highly specific DNA cleaving activity using the intein scaffold, we engineered the ACDs and characterized their homing site recognition. Protein engineering of the ACDs in the inteins illuminated a possible strategy for how inteins could avoid their extinction but spread via the acquisition of a diverse accessory domain.
PubMed: 35372505
DOI: 10.3389/fmolb.2022.855511
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.56 Å)
Structure validation

226707

건을2024-10-30부터공개중

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