Conservation of Structure and Mechanism between Eukaryotic Topoisomerase I and Site-Specific Recombinases Export

@article{citeulike:6045468, 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 α helices and a three-strand β 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.}, author = {Cheng, C.}, citeulike-article-id = {6045468}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0092-8674(00)81411-7}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0092-8674(00)81411-7}, doi = {10.1016/S0092-8674(00)81411-7}, issn = {00928674}, journal = {Cell}, keywords = {modeling, structure, topoisomerase}, month = {March}, number = {6}, pages = {841--850}, posted-at = {2009-10-30 23:48:29}, priority = {2}, title = {Conservation of Structure and Mechanism between Eukaryotic Topoisomerase I and Site-Specific Recombinases}, url = {http://dx.doi.org/10.1016/S0092-8674(00)81411-7}, volume = {92}, year = {1998} }

TY - JOUR ID - citeulike:6045468 L3 - citeulike-article-id:6045468 N2 - 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 α helices and a three-strand β 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. IS - 6 JF - Cell SN - 00928674 EP - 850 TI - Conservation of Structure and Mechanism between Eukaryotic Topoisomerase I and Site-Specific Recombinases VL - 92 SP - 841 KW - modeling KW - structure KW - topoisomerase AU - Cheng, C PY - 1998/03// UR - http://dx.doi.org/10.1016/S0092-8674(00)81411-7 ER -