1A41

TYPE 1-TOPOISOMERASE CATALYTIC FRAGMENT FROM VACCINIA VIRUS

Summary for 1A41

• Entry DOI: 10.2210/pdb1a41/pdb
• Descriptor: TOPOISOMERASE I, SULFATE ION (3 entities in total)
• Functional Keywords: type 1b topoisomerase, isomerase
• Biological source: Vaccinia virus
• Total number of polymer chains: 1
• Total formula weight: 27371.02

Authors

Cheng, C.,Kussie, P.,Pavletich, N.,Shuman, S. (deposition date: 1998-02-10, release date: 1999-06-01, Last modification date: 2024-02-07)

Primary citation

Cheng, C.,Kussie, P.,Pavletich, N.,Shuman, S.
Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases.
Cell(Cambridge,Mass.), 92:841-850, 1998

PubMed Abstract: Vaccinia DNA topoisomerase breaks and rejoins DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate. A C-terminal catalytic domain, Topo(81-314), suffices for transesterification chemistry. The domain contains a constellation of five amino acids, conserved in all eukaryotic type IB topoisomerases, that catalyzes attack of the tyrosine nucleophile on the scissile phosphate. The structure of the catalytic domain, consisting of ten alpha helices and a three-strand beta sheet, resembles the catalytic domains of site-specific recombinases that act via a topoisomerase IB-like mechanism. The topoisomerase catalytic pentad is conserved in the tertiary structures of the recombinases despite scant sequence similarity overall. This implies that the catalytic domains of type IB topoisomerases and recombinases derive from a common ancestral strand transferase.

PubMed: 9529259
DOI: 10.1016/S0092-8674(00)81411-7

Experimental method

X-RAY DIFFRACTION (2.3 Å)