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1mur

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(New page: 200px<br /><applet load="1mur" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mur, resolution 2.50&Aring;" /> '''TN5 TRANSPOSASE: 20M...)
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Revision as of 19:55, 24 November 2007

Image:1mur.gif

1mur, resolution 2.50Å

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TN5 TRANSPOSASE: 20MER OUTSIDE END 2 MN COMPLEX

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 Escherichia coli with MN as ligand. This structure superseeds the now removed PDB entry 1L1A. Full crystallographic information is available from 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:11896402

Page seeded by OCA on Sat Nov 24 22:02:40 2007

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