Structural highlights
Function
TNR6_ENTFL
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 integrase family of site-specific recombinases catalyze a diverse array of DNA rearrangements in archaebacteria, eubacteria and yeast. The solution structure of the DNA binding domain of the integrase protein from the conjugative transposon Tn916 has been determined using NMR spectroscopy. The structure provides the first insights into distal site DNA binding by a site-specific integrase and reveals that the N-terminal domain is structurally similar to the double stranded RNA binding domain (dsRBD). The results of chemical shift mapping experiments suggest that the integrase protein interacts with DNA using residues located on the face of its three stranded beta-sheet. This surface differs from the proposed RNA binding surface in dsRBDs, suggesting that different surfaces on the same protein fold can be used to bind DNA and RNA.
Site-specific DNA binding using a variation of the double stranded RNA binding motif.,Connolly KM, Wojciak JM, Clubb RT Nat Struct Biol. 1998 Jul;5(7):546-50. PMID:9665166[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Connolly KM, Wojciak JM, Clubb RT. Site-specific DNA binding using a variation of the double stranded RNA binding motif. Nat Struct Biol. 1998 Jul;5(7):546-50. PMID:9665166 doi:http://dx.doi.org/10.1038/799