1ecl: Difference between revisions

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[[Image:1ecl.~~gif~~|left|200px]]

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

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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).===

~~==Overview==~~

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~~The three~~-~~dimensional structure of the 67K amino~~-~~terminal fragment of Escherichia coli DNA topoisomerase I has been determined to 2.2 A resolution.~~ The ~~polypeptide folds in an unusual way to give four distinct domains enclosing a hole large enough to accommodate a double-stranded DNA. The active-site tyrosyl residue~~, ~~which is involved in~~ the ~~transient breakage of a DNA strand and~~ the ~~formation of a covalent enzyme-DNA intermediate, is present~~ at ~~the interface of two domains~~. ~~The structure suggests a plausible mechanism by which E~~. ~~coli DNA topoisomerase I and other members of the same DNA topoisomerase subfamily could catalyse~~ the ~~passage of one DNA strand through a transient break in another strand~~.

The line below this paragraph, {{ABSTRACT_PUBMED_8114910}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8114910 is the PubMed ID number.

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==About this Structure==

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[[Category: Dna cleavage]]

[[Category: Strand passage]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 14~~:56:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:29:52 2008''

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-[[Image:1ecl.gif|left|200px]]
+{{Seed}}
+[[Image:1ecl.png|left|200px]]
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 {{STRUCTURE_1ecl|  PDB=1ecl  |  SCENE=  }}
-'''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).===
-==Overview==
+<!--
-The three-dimensional structure of the 67K amino-terminal fragment of Escherichia coli DNA topoisomerase I has been determined to 2.2 A resolution. The polypeptide folds in an unusual way to give four distinct domains enclosing a hole large enough to accommodate a double-stranded DNA. The active-site tyrosyl residue, which is involved in the transient breakage of a DNA strand and the formation of a covalent enzyme-DNA intermediate, is present at the interface of two domains. The structure suggests a plausible mechanism by which E. coli DNA topoisomerase I and other members of the same DNA topoisomerase subfamily could catalyse the passage of one DNA strand through a transient break in another strand.
+The line below this paragraph, {{ABSTRACT_PUBMED_8114910}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8114910 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8114910}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Dna cleavage]]
 [[Category: Strand passage]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:56:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:29:52 2008''