1LWT

Crystal structure of the intein homing endonuclease PI-SceI bound to its substrate DNA (Ca2+ free)

Summary for 1LWT

• Entry DOI: 10.2210/pdb1lwt/pdb
• Related: 1LWS 1VDE
• Descriptor: PI-SceI DNA substrate top strand, PI-SceI DNA substrate bottom strand, ENDONUCLEASE PI-SCEI, ... (4 entities in total)
• Functional Keywords: homing endonuclease, protein-dna complex, intein, endonuclease, hydrolase-dna complex, hydrolase/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Endomembrane system: P17255
• Total number of polymer chains: 3
• Total formula weight: 74150.70

Authors

Moure, C.M.,Gimble, F.S.,Quiocho, F.A. (deposition date: 2002-06-03, release date: 2002-09-27, Last modification date: 2024-10-09)

Primary citation

Moure, C.M.,Gimble, F.S.,Quiocho, F.A.
Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence.
Nat.Struct.Biol., 9:764-770, 2002

PubMed Abstract: The first X-ray structures of an intein-DNA complex, that of the two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA substrate, have been determined in the presence and absence of Ca(2+). The DNA shows an asymmetric bending pattern, with a major 50 degree bend in the endonuclease domain and a minor 22 degree bend in the splicing domain region. Distortions of the DNA bound to the endonuclease domain cause the insertion of the two cleavage sites in the catalytic center. DNA binding induces changes in the protein conformation. The two overlapping non-identical active sites in the endonucleolytic center contain two Ca(+2) ions that coordinate to the catalytic Asp residues. Structure analysis indicates that the top strand may be cleaved first.

PubMed: 12219083
DOI: 10.1038/nsb840

Experimental method

X-RAY DIFFRACTION (3.2 Å)