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New page: left|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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[[Image:2bb8.gif|left|200px]]<br /><applet load="2bb8" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2bb8.gif|left|200px]]<br /><applet load="2bb8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2bb8" />
caption="2bb8" />
'''N-TERMINAL DNA BINDING DOMAIN FROM TN916 INTEGRASE, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
'''N-TERMINAL DNA BINDING DOMAIN FROM TN916 INTEGRASE, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />


==Overview==
==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.
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==
==About this Structure==
2BB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BB8 OCA].  
2BB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB8 OCA].  


==Reference==
==Reference==
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[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Clubb, R.T.]]
[[Category: Clubb, R T.]]
[[Category: Connolly, K.M.]]
[[Category: Connolly, K M.]]
[[Category: Wojciak, J.M.]]
[[Category: Wojciak, J M.]]
[[Category: dna binding]]
[[Category: dna binding]]
[[Category: dna recombination]]
[[Category: dna recombination]]
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[[Category: transposition]]
[[Category: transposition]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:41:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:55 2008''