Structural highlights
Function
Q6D6K1_PECAS
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structures of the N-terminal domains of two integrases of closely related but not identical asn tDNA-associated genomic islands, Yersinia HPI (high pathogenicity island; encoding siderophore yersiniabactin biosynthesis and transport) and an Erwinia carotovora genomic island with yet unknown function, HAI7, have been resolved. Both integrases utilize a novel four-stranded beta-sheet DNA-binding motif, in contrast to the known proteins that bind their DNA targets by means of three-stranded beta-sheets. Moreover, the beta-sheets in Int(HPI) and Int(HAI7) are longer than those in other integrases, and the structured helical N terminus is positioned perpendicularly to the large C-terminal helix. These differences strongly support the proposal that the integrases of the genomic islands make up a distinct evolutionary branch of the site-specific recombinases that utilize a unique DNA-binding mechanism.
Structures of the arm-type binding domains of HPI and HAI7 integrases.,Szwagierczak A, Antonenka U, Popowicz GM, Sitar T, Holak TA, Rakin A J Biol Chem. 2009 Nov 13;284(46):31664-71. Epub 2009 Sep 8. PMID:19737930[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Szwagierczak A, Antonenka U, Popowicz GM, Sitar T, Holak TA, Rakin A. Structures of the arm-type binding domains of HPI and HAI7 integrases. J Biol Chem. 2009 Nov 13;284(46):31664-71. Epub 2009 Sep 8. PMID:19737930 doi:10.1074/jbc.M109.059261