1b69

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1b69" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b69" /> '''THE SOLUTION STRUCTURE OF TN916 INTEGRASE N-...)
Line 1: Line 1:
-
[[Image:1b69.gif|left|200px]]<br /><applet load="1b69" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1b69.gif|left|200px]]<br /><applet load="1b69" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b69" />
caption="1b69" />
'''THE SOLUTION STRUCTURE OF TN916 INTEGRASE N-TERMINAL DOMAIN/DNA COMPLEX'''<br />
'''THE SOLUTION STRUCTURE OF TN916 INTEGRASE N-TERMINAL DOMAIN/DNA COMPLEX'''<br />
==Overview==
==Overview==
-
The integrase protein catalyzes the excision and integration of the Tn916, conjugative transposon, a promiscuous genetic element that spreads, antibiotic resistance in pathogenic bacteria. The solution structure of, the N-terminal domain of the Tn916 integrase protein bound to its, DNA-binding site within the transposon arm has been determined. The, structure reveals an interesting mode of DNA recognition, in which the, face of a three-stranded antiparallel beta-sheet is positioned within the, major groove. A comparison to the structure of the homing endonuclease, I-Ppol-DNA complex suggests that the three-stranded sheet may represent a, new DNA-binding motif whose residue composition and position within the, major groove are varied to alter specificity. The structure also provides, insights into the mechanism of conjugative transposition. The DNA in the, complex is bent approximately 35 degrees and may, together with potential, interactions between bound integrase proteins at directly repeated sites, significantly bend the arms of the transposon.
+
The integrase protein catalyzes the excision and integration of the Tn916 conjugative transposon, a promiscuous genetic element that spreads antibiotic resistance in pathogenic bacteria. The solution structure of the N-terminal domain of the Tn916 integrase protein bound to its DNA-binding site within the transposon arm has been determined. The structure reveals an interesting mode of DNA recognition, in which the face of a three-stranded antiparallel beta-sheet is positioned within the major groove. A comparison to the structure of the homing endonuclease I-Ppol-DNA complex suggests that the three-stranded sheet may represent a new DNA-binding motif whose residue composition and position within the major groove are varied to alter specificity. The structure also provides insights into the mechanism of conjugative transposition. The DNA in the complex is bent approximately 35 degrees and may, together with potential interactions between bound integrase proteins at directly repeated sites, significantly bend the arms of the transposon.
==About this Structure==
==About this Structure==
-
1B69 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=1B69 OCA].
+
1B69 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=1B69 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[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: beta-sheet recognition]]
[[Category: beta-sheet recognition]]
[[Category: complex]]
[[Category: complex]]
Line 22: Line 22:
[[Category: transposition]]
[[Category: transposition]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:23:44 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:01 2008''

Revision as of 09:52, 21 February 2008


1b69

Drag the structure with the mouse to rotate

THE SOLUTION STRUCTURE OF TN916 INTEGRASE N-TERMINAL DOMAIN/DNA COMPLEX

Overview

The integrase protein catalyzes the excision and integration of the Tn916 conjugative transposon, a promiscuous genetic element that spreads antibiotic resistance in pathogenic bacteria. The solution structure of the N-terminal domain of the Tn916 integrase protein bound to its DNA-binding site within the transposon arm has been determined. The structure reveals an interesting mode of DNA recognition, in which the face of a three-stranded antiparallel beta-sheet is positioned within the major groove. A comparison to the structure of the homing endonuclease I-Ppol-DNA complex suggests that the three-stranded sheet may represent a new DNA-binding motif whose residue composition and position within the major groove are varied to alter specificity. The structure also provides insights into the mechanism of conjugative transposition. The DNA in the complex is bent approximately 35 degrees and may, together with potential interactions between bound integrase proteins at directly repeated sites, significantly bend the arms of the transposon.

About this Structure

1B69 is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.

Reference

NMR structure of the Tn916 integrase-DNA complex., Wojciak JM, Connolly KM, Clubb RT, Nat Struct Biol. 1999 Apr;6(4):366-73. PMID:10201406

Page seeded by OCA on Thu Feb 21 11:52:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools