Plasmodium falciparum UvrD Helicase Translocates in 3′ to 5′ Direction, Colocalizes with MLH and Modulates Its Activity through Physical Interaction
Figure 2
Schematic diagrams showing the domain organization. A,
E. coli and B, P. falciparum UvrD helicases. Domain analysis was done using Scan Prosite at (http://expasy.org). The domain structure was taken from the results and used in the figures. UvrD helicase ATP binding and UvrD C-terminal domains are shown. The numbers show the amino acids spanning these motifs. C, The detailed domain organization of P. falciparum UvrD helicase. The conserved sequences of each domain are written inside the boxes. The text in blue refers to the names of various conserved domains and the numbers refer to the amino acids separating the various domains and the length of N- and C-terminal extensions. This figure is not drawn to scale. D–F, The detailed domain structure of PfUDN, PfUDC1 and PfUDC2 fragments of P. falciparum UvrD. The details are as in C. The colored lines are same as in Figure 1 and correspond to domain 1A, 1B, 2A and 2B present in PfUDN, PfUDC1 and PfUDC2 respectively. (G–I) Structure modeling. The PfUvrD full-length sequence was submitted to Swissmodel server and the structure was obtained. The molecular graphic images were produced using the UCSF Chimera package from the resource for Biocomputing, Visualization, and Informatics (http://www.cgl.ucsf.edu/chimera) at the University of California, San Francisco (supported by NIH P41 RR-01081). G. Template; H. full-length PfUvrD; I. superimposed image.