1VDE

PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY

Summary for 1VDE

• Entry DOI: 10.2210/pdb1vde/pdb
• Descriptor: PI-SCEI (2 entities in total)
• Functional Keywords: homing endonuclease, protein splicing, endonuclease
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Endomembrane system: P17255
• Total number of polymer chains: 2
• Total formula weight: 102007.79

Authors

Duan, X.,Quiocho, F.A. (deposition date: 1997-04-01, release date: 1998-04-08, Last modification date: 2024-02-14)

Primary citation

Duan, X.,Gimble, F.S.,Quiocho, F.A.
Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity.
Cell(Cambridge,Mass.), 89:555-564, 1997

PubMed Abstract: PI-Scel is a bifunctional yeast protein that propagates its mobile gene by catalyzing protein splicing and site-specific DNA double-strand cleavage. Here, we report the 2.4 A crystal structure of the PI-Scel protein. The structure is composed of two separate domains (I and II) with novel folds and different functions. Domain I, which is elongated and formed largely from seven beta sheets, harbors the N and C termini residues and two His residues that are implicated in protein splicing. Domain II, which is compact and is primarily composed of two similar alpha/beta motifs related by local two-fold symmetry, contains the putative nuclease active site with a cluster of two acidic residues and one basic residue commonly found in restriction endonucleases. This report presents prototypic structures of domains with single endonuclease and protein splicing active sites.

PubMed: 9160747
DOI: 10.1016/S0092-8674(00)80237-8

Experimental method

X-RAY DIFFRACTION (2.4 Å)