1mur
From Proteopedia
(New page: 200px<br /><applet load="1mur" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mur, resolution 2.50Å" /> '''TN5 TRANSPOSASE: 20M...) |
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| - | [[Image:1mur.gif|left|200px]]<br /><applet load="1mur" size=" | + | [[Image:1mur.gif|left|200px]]<br /><applet load="1mur" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mur, resolution 2.50Å" /> | caption="1mur, resolution 2.50Å" /> | ||
'''TN5 TRANSPOSASE: 20MER OUTSIDE END 2 MN COMPLEX'''<br /> | '''TN5 TRANSPOSASE: 20MER OUTSIDE END 2 MN COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A synaptic complex of Tn5 transposase with an extended outside end DNA | + | 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== | ==About this Structure== | ||
| - | 1MUR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1MUR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1L1A. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Goryshin, I | + | [[Category: Goryshin, I Y.]] |
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
[[Category: Lovell, S.]] | [[Category: Lovell, S.]] | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Reznikoff, W | + | [[Category: Reznikoff, W R.]] |
| - | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
[[Category: transposase]] | [[Category: transposase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:14 2008'' |
Revision as of 11:59, 21 February 2008
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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 as ligand. This structure supersedes 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
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