6RPQ
Crystal structure of PhoCDC21-1 intein
Summary for 6RPQ
| Entry DOI | 10.2210/pdb6rpq/pdb |
| Descriptor | Ubiquitin-like protein SMT3,1108aa long hypothetical cell division control protein (1 entity in total) |
| Functional Keywords | intein, protein-splicing, hint, hydrolase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 1 |
| Total formula weight | 32263.50 |
| Authors | Beyer, H.M.,Mikula, K.M.,Iwai, H. (deposition date: 2019-05-14, release date: 2019-08-14, Last modification date: 2024-01-24) |
| Primary citation | Beyer, H.M.,Mikula, K.M.,Kudling, T.V.,Iwai, H. Crystal structures of CDC21-1 inteins from hyperthermophilic archaea reveal the selection mechanism for the highly conserved homing endonuclease insertion site. Extremophiles, 23:669-679, 2019 Cited by PubMed Abstract: Self-splicing inteins are mobile genetic elements invading host genes via nested homing endonuclease (HEN) domains. All HEN domains residing within inteins are inserted at a highly conserved insertion site. A purifying selection mechanism directing the location of the HEN insertion site has not yet been identified. In this work, we solved the three-dimensional crystal structures of two inteins inserted in the cell division control protein 21 of the hyperthermophilic archaea Pyrococcus abyssi and Pyrococcus horikoshii. A comparison between the structures provides the structural basis for the thermo-stabilization mechanism of inteins that have lost the HEN domain during evolution. The presence of an entire extein domain in the intein structure from Pyrococcus horikoshii suggests the selection mechanism for the highly conserved HEN insertion point. PubMed: 31363851DOI: 10.1007/s00792-019-01117-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.654 Å) |
Structure validation
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