1ecl: Difference between revisions

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[[Image:1ecl.png|left|200px]]
[[Image:1ecl.png|left|200px]]


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{{STRUCTURE_1ecl|  PDB=1ecl  |  SCENE=  }}  
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===AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1).===
===AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1).===


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{{ABSTRACT_PUBMED_8114910}}
{{ABSTRACT_PUBMED_8114910}}


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==See Also==
==See Also==
*[[Topoisomerase]]
*[[Topoisomerase|Topoisomerase]]


==Reference==
==Reference==
<ref group="xtra">PMID:8114910</ref><references group="xtra"/>
<ref group="xtra">PMID:008114910</ref><references group="xtra"/>
[[Category: DNA topoisomerase]]
[[Category: DNA topoisomerase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]

Revision as of 01:25, 27 July 2012

File:1ecl.png

Template:STRUCTURE 1ecl

AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1).AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1).

Template:ABSTRACT PUBMED 8114910

About this StructureAbout this Structure

1ecl is a 1 chain structure of Topoisomerase with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Lima CD, Wang JC, Mondragon A. Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I. Nature. 1994 Jan 13;367(6459):138-46. PMID:8114910 doi:http://dx.doi.org/10.1038/367138a0

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OCA