1mus
From Proteopedia
(New page: 200px<br /> <applet load="1mus" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mus, resolution 1.90Å" /> '''crystal structure o...) |
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| - | [[Image:1mus.gif|left|200px]]<br /> | + | [[Image:1mus.gif|left|200px]]<br /><applet load="1mus" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mus" size=" | + | |
caption="1mus, resolution 1.90Å" /> | caption="1mus, resolution 1.90Å" /> | ||
'''crystal structure of Tn5 transposase complexed with resolved outside end DNA'''<br /> | '''crystal structure of Tn5 transposase complexed with resolved outside end DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Prokaryotic transposon 5 (Tn5) serves as a model system for studying the | + | Prokaryotic transposon 5 (Tn5) serves as a model system for studying the molecular mechanism of DNA transposition. Elucidation of the X-ray co-crystal structure of Tn5 transposase complexed with a DNA recognition end sequence provided the first three-dimensional picture of an intermediate in a transposition/retroviral integration pathway. The many Tn5 transposase-DNA co-crystal structures now available complement biochemical and genetic studies, allowing a comprehensive and detailed understanding of transposition mechanisms. Specifically, the structures reveal two different types of protein-DNA contacts: cis contacts, required for initial DNA recognition, and trans contacts, required for catalysis. Protein-protein contacts required for synapsis are also seen. Finally, the two divalent metals in the active site of the transposase support a 'two-metal-ion' mechanism for Tn5 transposition. |
==About this Structure== | ==About this Structure== | ||
| - | 1MUS 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, MG and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1MUS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb84_1.html Transposase]]. Full crystallographic information is available from [http:// | + | 1MUS 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>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1MUS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb84_1.html Transposase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Transposase]] | [[Category: Transposase]] | ||
| - | [[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 S.]] |
[[Category: Steiniger-White, M.]] | [[Category: Steiniger-White, M.]] | ||
| - | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: transposase]] | [[Category: transposase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:13 2008'' |
Revision as of 11:59, 21 February 2008
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crystal structure of Tn5 transposase complexed with resolved outside end DNA
Overview
Prokaryotic transposon 5 (Tn5) serves as a model system for studying the molecular mechanism of DNA transposition. Elucidation of the X-ray co-crystal structure of Tn5 transposase complexed with a DNA recognition end sequence provided the first three-dimensional picture of an intermediate in a transposition/retroviral integration pathway. The many Tn5 transposase-DNA co-crystal structures now available complement biochemical and genetic studies, allowing a comprehensive and detailed understanding of transposition mechanisms. Specifically, the structures reveal two different types of protein-DNA contacts: cis contacts, required for initial DNA recognition, and trans contacts, required for catalysis. Protein-protein contacts required for synapsis are also seen. Finally, the two divalent metals in the active site of the transposase support a 'two-metal-ion' mechanism for Tn5 transposition.
About this Structure
1MUS is a Single protein structure of sequence from Escherichia coli with , and as ligands. The following page contains interesting information on the relation of 1MUS with [Transposase]. Full crystallographic information is available from OCA.
Reference
Structure/function insights into Tn5 transposition., Steiniger-White M, Rayment I, Reznikoff WS, Curr Opin Struct Biol. 2004 Feb;14(1):50-7. PMID:15102449
Page seeded by OCA on Thu Feb 21 13:59:13 2008
Categories: Escherichia coli | Single protein | Transposase | Holden, H M. | Lovell, S. | Rayment, I. | Reznikoff, W S. | Steiniger-White, M. | Thoden, J B. | EDO | MG | MN | Dna binding | Hairpin
