2f7t: Difference between revisions

Line 4:

==Overview==

We present the crystal structure of the catalytic domain of Mos1, transposase, a member of the Tc1/mariner family of transposases. The, structure comprises an RNase H-like core, bringing together an aspartic, acid triad to form the active site, capped by N- and C-terminal, alpha-helices. We have solved structures with either one Mg2+ or two Mn2+, ions in the active site, consistent with a two-metal mechanism for, catalysis. The lack of hairpin-stabilizing structural motifs is consistent, with the absence of a hairpin intermediate in Mos1 excision. We have built, a model for the DNA-binding domain of Mos1 transposase, based on the, structure of the bipartite DNA-binding domain of Tc3 transposase., Combining this with the crystal structure of the catalytic domain provides, a model for the paired-end complex formed between a dimer of Mos1, transposase and inverted repeat DNA. The implications for the mechanisms, of first and second strand cleavage are discussed.

We present the crystal structure of the catalytic domain of Mos1 transposase, a member of the Tc1/mariner family of transposases. The structure comprises an RNase H-like core, bringing together an aspartic acid triad to form the active site, capped by N- and C-terminal alpha-helices. We have solved structures with either one Mg2+ or two Mn2+ ions in the active site, consistent with a two-metal mechanism for catalysis. The lack of hairpin-stabilizing structural motifs is consistent with the absence of a hairpin intermediate in Mos1 excision. We have built a model for the DNA-binding domain of Mos1 transposase, based on the structure of the bipartite DNA-binding domain of Tc3 transposase. Combining this with the crystal structure of the catalytic domain provides a model for the paired-end complex formed between a dimer of Mos1 transposase and inverted repeat DNA. The implications for the mechanisms of first and second strand cleavage are discussed.

==About this Structure==

Line 14:

[[Category: Single protein]]

[[Category: Dawson, A.]]

[[Category: Finnegan, D.J.]]

[[Category: Finnegan, D J.]]

[[Category: Richardson, J.M.]]

[[Category: Richardson, J M.]]

[[Category: Taylor, P.]]

[[Category: Walkinshaw, M.D.]]

[[Category: Walkinshaw, M D.]]

[[Category: MG]]

[[Category: ddd motif]]

[[Category: rnase-h like fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jan 29 19~~:29:34 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:18:38 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-We present the crystal structure of the catalytic domain of Mos1, transposase, a member of the Tc1/mariner family of transposases. The, structure comprises an RNase H-like core, bringing together an aspartic, acid triad to form the active site, capped by N- and C-terminal, alpha-helices. We have solved structures with either one Mg2+ or two Mn2+, ions in the active site, consistent with a two-metal mechanism for, catalysis. The lack of hairpin-stabilizing structural motifs is consistent, with the absence of a hairpin intermediate in Mos1 excision. We have built, a model for the DNA-binding domain of Mos1 transposase, based on the, structure of the bipartite DNA-binding domain of Tc3 transposase., Combining this with the crystal structure of the catalytic domain provides, a model for the paired-end complex formed between a dimer of Mos1, transposase and inverted repeat DNA. The implications for the mechanisms, of first and second strand cleavage are discussed.
+We present the crystal structure of the catalytic domain of Mos1 transposase, a member of the Tc1/mariner family of transposases. The structure comprises an RNase H-like core, bringing together an aspartic acid triad to form the active site, capped by N- and C-terminal alpha-helices. We have solved structures with either one Mg2+ or two Mn2+ ions in the active site, consistent with a two-metal mechanism for catalysis. The lack of hairpin-stabilizing structural motifs is consistent with the absence of a hairpin intermediate in Mos1 excision. We have built a model for the DNA-binding domain of Mos1 transposase, based on the structure of the bipartite DNA-binding domain of Tc3 transposase. Combining this with the crystal structure of the catalytic domain provides a model for the paired-end complex formed between a dimer of Mos1 transposase and inverted repeat DNA. The implications for the mechanisms of first and second strand cleavage are discussed.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Dawson, A.]]
-[[Category: Finnegan, D.J.]]
+[[Category: Finnegan, D J.]]
-[[Category: Richardson, J.M.]]
+[[Category: Richardson, J M.]]
 [[Category: Taylor, P.]]
-[[Category: Walkinshaw, M.D.]]
+[[Category: Walkinshaw, M D.]]
 [[Category: MG]]
 [[Category: ddd motif]]
 [[Category: rnase-h like fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:29:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:18:38 2008''