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1vde
From Proteopedia
Revision as of 21:26, 29 September 2014 by OCA (Talk | contribs)
1vde is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity.,Duan X, Gimble FS, Quiocho FA Cell. 1997 May 16;89(4):555-64. PMID:9160747[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Duan X, Gimble FS, Quiocho FA. Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Cell. 1997 May 16;89(4):555-64. PMID:9160747
