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7OEC

Crystal structure of an intein from a hyperthermophile

Summary for 7OEC
Entry DOI10.2210/pdb7oec/pdb
DescriptorDNA polymerase II large subunit, SULFATE ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
Functional Keywordsprotein splicing, intein, splicing
Biological sourcePyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Total number of polymer chains1
Total formula weight19989.37
Authors
Hannes, B.,Hiltunen, M.,Iwai, H. (deposition date: 2021-05-03, release date: 2021-05-26, Last modification date: 2024-11-13)
Primary citationHiltunen, M.K.,Beyer, H.M.,Iwai, H.
Mini-Intein Structures from Extremophiles Suggest a Strategy for Finding Novel Robust Inteins.
Microorganisms, 9:-, 2021
Cited by
PubMed Abstract: Inteins are prevalent among extremophiles. Mini-inteins with robust splicing properties are of particular interest for biotechnological applications due to their small size. However, biochemical and structural characterization has still been limited to a small number of inteins, and only a few serve as widely used tools in protein engineering. We determined the crystal structure of a naturally occurring Pol-II mini-intein from and compared all three mini-inteins found in the genome of . Despite their similar sizes, the comparison revealed distinct differences in the insertions and deletions, implying specific evolutionary pathways from distinct ancestral origins. Our studies suggest that sporadically distributed mini-inteins might be more promising for further protein engineering applications than highly conserved mini-inteins. Structural investigations of additional inteins could guide the shortest path to finding novel robust mini-inteins suitable for various protein engineering purposes.
PubMed: 34198729
DOI: 10.3390/microorganisms9061226
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.48 Å)
Structure validation

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