Structures of the arm-type binding domains of HPI and HAI7 integrases.
J Biol Chem
; 284(46): 31664-71, 2009 Nov 13.
Article
in En
| MEDLINE
| ID: mdl-19737930
ABSTRACT
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Yersinia pestis
/
Integrases
/
Genomic Islands
Language:
En
Journal:
J Biol Chem
Year:
2009
Document type:
Article
Affiliation country:
Germany