Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase. Export

@article{citeulike:3870659, abstract = {The bifunctional enzyme dihydrofolate reductase-thymidylate synthase catalyses both the reductive methylation of 2'-deoxyuridylate and the subsequent reduction of dihydrofolate to yield 2'-deoxythymidylate and tetrahydrofolate at two spacially discrete sites situated on different protein domains. The X-ray structure of dihydrofolate reductase-thymidylate synthase from Leishmania major indicates that transfer of dihydrofolate between these sites does not occur by transient binding at both sites but rather by movement of dihydrofolate across the surface of the protein. The enzyme has an unusual surface charge distribution that could account for this channelling of dihydrofolate between active sites.}, author = {Knighton, D. R. and Kan, C. C. and Howland, E. and Janson, C. A. and Hostomska, Z. and Welsh, K. M. and Matthews, D. A.}, citeulike-article-id = {3870659}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/7656037}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=7656037}, issn = {1072-8368}, journal = {Nature structural biology}, keywords = {channeling, channelingexample, electrostatic}, month = {March}, number = {3}, pages = {186--194}, posted-at = {2009-01-09 05:50:22}, priority = {2}, title = {Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/7656037}, volume = {1}, year = {1994} }

TY - JOUR ID - citeulike:3870659 L3 - citeulike-article-id:3870659 N2 - The bifunctional enzyme dihydrofolate reductase-thymidylate synthase catalyses both the reductive methylation of 2'-deoxyuridylate and the subsequent reduction of dihydrofolate to yield 2'-deoxythymidylate and tetrahydrofolate at two spacially discrete sites situated on different protein domains. The X-ray structure of dihydrofolate reductase-thymidylate synthase from Leishmania major indicates that transfer of dihydrofolate between these sites does not occur by transient binding at both sites but rather by movement of dihydrofolate across the surface of the protein. The enzyme has an unusual surface charge distribution that could account for this channelling of dihydrofolate between active sites. IS - 3 JF - Nature structural biology SN - 1072-8368 EP - 194 TI - Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase. VL - 1 SP - 186 KW - channeling KW - channelingexample KW - electrostatic AU - Knighton, DR AU - Kan, CC AU - Howland, E AU - Janson, CA AU - Hostomska, Z AU - Welsh, KM AU - Matthews, DA PY - 1994/03// UR - http://view.ncbi.nlm.nih.gov/pubmed/7656037 ER -