1ecl: Difference between revisions
New page: left|200px<br /><applet load="1ecl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ecl, resolution 1.9Å" /> '''AMINO TERMINAL 67KDA ... |
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[[Image:1ecl.gif|left|200px]]<br /><applet load="1ecl" size=" | [[Image:1ecl.gif|left|200px]]<br /><applet load="1ecl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ecl, resolution 1.9Å" /> | caption="1ecl, resolution 1.9Å" /> | ||
'''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).'''<br /> | '''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).'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of the 67K amino-terminal fragment of | 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. | ||
==About this Structure== | ==About this Structure== | ||
1ECL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] Full crystallographic information is available from [http:// | 1ECL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lima, C | [[Category: Lima, C D.]] | ||
[[Category: Mondragon, A.]] | [[Category: Mondragon, A.]] | ||
[[Category: Wang, J | [[Category: Wang, J C.]] | ||
[[Category: bacterial type i]] | [[Category: bacterial type i]] | ||
[[Category: dna cleavage]] | [[Category: dna cleavage]] | ||
[[Category: strand passage]] | [[Category: strand passage]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:19 2008'' | ||
Revision as of 13:26, 21 February 2008
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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).
OverviewOverview
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.
About this StructureAbout this Structure
1ECL is a Single protein structure of sequence from Escherichia coli. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I., Lima CD, Wang JC, Mondragon A, Nature. 1994 Jan 13;367(6459):138-46. PMID:8114910
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