1mur: Difference between revisions

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[[Image:1mur.~~gif~~|left|200px]]

[[Image:1mur.png|left|200px]]

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~~==Overview==~~

A synaptic complex of Tn5 transposase with an extended outside end DNA duplex was prepared and crystallized, and its crystal structure was determined in an effort to reveal the role of metal ions in catalysis. Two Mn2+ ions bound to the active site when a single nucleotide of donor DNA was added to the 3' end of the transferred strand. Marked conformational changes were observed in the DNA bases closest to the active site. The position of the metal ions and the conformational changes of the DNA provide insight into the mechanism of hairpin formation and cleavage, and is consistent with a two-metal model for catalysis.

==About this Structure==

1MUR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUR OCA].

~~==Reference==~~

Two-metal active site binding of a Tn5 transposase synaptic complex., Lovell S, Goryshin IY, Reznikoff WR, Rayment I, Nat Struct Biol. 2002 Apr;9(4):278-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11896402 11896402]

[[Category: Escherichia coli]]

[[Category: Single protein]]

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[[Category: Dna binding]]

[[Category: Transposase]]

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-[[Image:1mur.gif|left|200px]]
+[[Image:1mur.png|left|200px]]
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-==Overview==
+{{ABSTRACT_11896402}}
-A synaptic complex of Tn5 transposase with an extended outside end DNA duplex was prepared and crystallized, and its crystal structure was determined in an effort to reveal the role of metal ions in catalysis. Two Mn2+ ions bound to the active site when a single nucleotide of donor DNA was added to the 3' end of the transferred strand. Marked conformational changes were observed in the DNA bases closest to the active site. The position of the metal ions and the conformational changes of the DNA provide insight into the mechanism of hairpin formation and cleavage, and is consistent with a two-metal model for catalysis.
 ==About this Structure==
 MUR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUR OCA].
-==Reference==
-Two-metal active site binding of a Tn5 transposase synaptic complex., Lovell S, Goryshin IY, Reznikoff WR, Rayment I, Nat Struct Biol. 2002 Apr;9(4):278-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11896402 11896402]
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
@@ Line 30: / Line 26: @@
 [[Category: Dna binding]]
 [[Category: Transposase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:44:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 19:20:21 2008''