2bb8
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(New page: 200px<br /><applet load="2bb8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bb8" /> '''N-TERMINAL DNA BINDING DOMAIN FROM TN916 INT...)
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Revision as of 06:34, 21 November 2007
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N-TERMINAL DNA BINDING DOMAIN FROM TN916 INTEGRASE, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
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.
About this Structure
2BB8 is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.
Reference
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
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