6rpp | pdb_00006rpp

Crystal structure of PabCDC21-1 intein

spinqualitylabelsall models 6rpp, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rpp is a 1 chain structure with sequence from Pyrococcus abyssi GE5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: ACT, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9UYR7_PYRAB Publication Abstract from PubMed 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. Crystal structures of CDC21-1 inteins from hyperthermophilic archaea reveal the selection mechanism for the highly conserved homing endonuclease insertion site.,Beyer HM, Mikula KM, Kudling TV, Iwai H Extremophiles. 2019 Jul 30. pii: 10.1007/s00792-019-01117-4. doi:, 10.1007/s00792-019-01117-4. PMID:31363851 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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