2vic: Difference between revisions

Revision as of 18:51, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2vic.png

Template:STRUCTURE 2vic

CRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX WITH LEFT END 26-MER DNA AND MANGANESECRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX WITH LEFT END 26-MER DNA AND MANGANESE

Template:ABSTRACT PUBMED 18243097

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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OCA

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-[[Image:2vic.jpg|left|200px]]
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 {{STRUCTURE_2vic|  PDB=2vic  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX WITH LEFT END 26-MER DNA AND MANGANESE'''
+===CRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX WITH LEFT END 26-MER DNA AND MANGANESE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18243097}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18243097 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18243097}}
 ==About this Structure==
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 [[Category: Protein-dna complex]]
 [[Category: Transposition]]
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