@article{mbs:/content/journal/jgv/10.1099/0022-1317-76-12-2949, author = "Raj, Kenneth and Stanley, M. A.", title = "The ATP-binding and ATPase activities of human papillomavirus type 16 E1 are significantly weakened by the absence of prolines in its ATP-binding domain", journal= "Journal of General Virology", year = "1995", volume = "76", number = "12", pages = "2949-2956", doi = "https://doi.org/10.1099/0022-1317-76-12-2949", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-76-12-2949", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The E1 protein of human papillomavirus (HPV) type 16 is the only known papillomavirus E1 which does not contain any proline residues in the phosphate-loop (P-loop) of its ATP-binding site. To ascertain whether this feature influences the activities of HPV-16 E1, we generated a mutant HPV-16 E1 (E1Pro) in which prolines are inserted in place of alanines in this site, making the P-loop identical to its bovine papillomavirus type 1 counterpart. Glutathione S-transferase (GST) fusion proteins (GSTE1wt and GSTE1Pro) were produced, purified and used to assay for ATP-binding ability, ATPase activity and ability to complex with the HPV-16 E2 protein. The results show that the lack of prolines in the P-loop, which is unique to HPV-16 E1, significantly weakens its ATP-binding and ATPase activities without affecting its ability to complex with the HPV-16 E2 protein.", }