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).

1ECL の概要

• エントリーDOI: 10.2210/pdb1ecl/pdb
• 分子名称: ESCHERICHIA COLI TOPOISOMERASE I (2 entities in total)
• 機能のキーワード: bacterial type i, dna cleavage, strand passage, topoisomerase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67326.30

構造登録者

Lima, C.D.,Wang, J.C.,Mondragon, A. (登録日: 1995-05-05, 公開日: 1995-07-31, 最終更新日: 2024-02-07)

主引用文献

Lima, C.D.,Wang, J.C.,Mondragon, A.
Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I.
Nature, 367:138-146, 1994

PubMed Abstract: 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.

PubMed: 8114910
DOI: 10.1038/367138a0

実験手法

X-RAY DIFFRACTION (1.9 Å)