2vic: Difference between revisions
New page: left|200px<br /><applet load="2vic" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vic, resolution 2.35Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:2vic.jpg|left|200px]] | [[Image:2vic.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX WITH LEFT END 26-MER DNA AND MANGANESE''' | {{Structure | ||
|PDB= 2vic |SIZE=350|CAPTION= <scene name='initialview01'>2vic</scene>, resolution 2.35Å | |||
|SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Mn+Binding+Site+For+Chain+D'>AC2</scene> | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX WITH LEFT END 26-MER DNA AND MANGANESE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2VIC is a [ | 2VIC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIC OCA]. | ||
==Reference== | ==Reference== | ||
Mechanism of IS200/IS605 Family DNA Transposases: Activation and Transposon-Directed Target Site Selection., Barabas O, Ronning DR, Guynet C, Hickman AB, Ton-Hoang B, Chandler M, Dyda F, Cell. 2008 Jan 25;132(2):208-20. PMID:[http:// | Mechanism of IS200/IS605 Family DNA Transposases: Activation and Transposon-Directed Target Site Selection., Barabas O, Ronning DR, Guynet C, Hickman AB, Ton-Hoang B, Chandler M, Dyda F, Cell. 2008 Jan 25;132(2):208-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18243097 18243097] | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transposition]] | [[Category: transposition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:46:52 2008'' | ||
Revision as of 19:46, 20 March 2008
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CRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX WITH LEFT END 26-MER DNA AND MANGANESE
OverviewOverview
The smallest known DNA transposases are those from the IS200/IS605 family. Here we show how the interplay of protein and DNA activates TnpA, the Helicobacter pylori IS608 transposase, for catalysis. First, transposon end binding causes a conformational change that aligns catalytically important protein residues within the active site. Subsequent precise cleavage at the left and right ends, the steps that liberate the transposon from its donor site, does not involve a site-specific DNA-binding domain. Rather, cleavage site recognition occurs by complementary base pairing with a TnpA-bound subterminal transposon DNA segment. Thus, the enzyme active site is constructed from elements of both protein and DNA, reminiscent of the interdependence of protein and RNA in the ribosome. Our structural results explain why the transposon ends are asymmetric and how the transposon selects a target site for integration, and they allow us to propose a molecular model for the entire transposition reaction.
About this StructureAbout this Structure
2VIC is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of IS200/IS605 Family DNA Transposases: Activation and Transposon-Directed Target Site Selection., Barabas O, Ronning DR, Guynet C, Hickman AB, Ton-Hoang B, Chandler M, Dyda F, Cell. 2008 Jan 25;132(2):208-20. PMID:18243097
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