Biography
Jaroslaw Blaszczyk has completed his PhD at the age of 30 years from Technical University of Lodz and postdoctoral studies from NIH, National Cancer Institute at Frederick. He became a research assistant professor at Michigan State University. After that he served as the PDB annotator at Rutgers University of New Jersey. Currently he is an assistant professor at the Centre of Molecular and Macromolecular Studies of the Polish Academy of Sciences. He has published more than 67 papers in reputed journals and has been serving at several grant review panels at NCN, the Polish National Science Center.
Abstract
RNase III endonucleases cleave double-stranded RNA, transforming precursor RNAs into mature RNAs that act in pre-mRNA splicing, RNA modification, translation, gene silencing, and the regulation of developmental timing. The structure of endonuclease domain, determined, by author, in 2001, provided, first time after 33 years from first isolation of the enzyme, a hint at how this family of ribonucleases functions. First structure of full-length, unligated RNase III, was solved in 2002. First structure of full-length enzyme in complex with dsRNA was solved, by author, in 2004. After that, a significant number of RNase III structures in complex with dsRNA variants were determined. The \'key\' structure is an enzyme-product complex, published in Cell in 2006. The following years resulted in determination of the large variety of RNase III structures: from different organisms, in form of a complex with different dsRNAs, metal ions, and/or other entities. All these structures constitute a set of snapshots of the mechanism of double-stranded RNA processing by the enzyme. \r\nThis presentation is dedicated to Professor Wojciech J. Stec on the occasion of his 75th birthday. Financial support by the Polish National Science Center (NCN), grant No. DEC-2012/05/B/ST4/00075, is gratefully acknowledged.\r\n
Biography
Jaroslaw Blaszczyk has completed his PhD at the age of 30 years from Technical University of Lodz and postdoctoral studies from NIH, National Cancer Institute at Frederick. He became a research assistant professor at Michigan State University. After that he served as the PDB annotator at Rutgers University of New Jersey. Currently he is an assistant professor at the Centre of Molecular and Macromolecular Studies of the Polish Academy of Sciences. He has published more than 67 papers in reputed journals and has been serving at several grant review panels at NCN, the Polish National Science Center.
Abstract
We discovered the new, hexagonal crystal form of lipase B from Candida antarctica (CAL-B). The NAG (N-acetyl-D-glucosamine) molecules, which were closing the glycosylation site in the orthorhombic form, in our hexagonal structure, unexpectedly, adopt an open conformation. We do not know whether the opening and closing of the glycosylation site by the ‘lid’ NAG moiety, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release.\r\nThe packing of molecules in the hexagonal crystal makes the active center of the enzyme very well accessible for the ligand, which, in our opinion, may help in the enzyme-ligand complex formation.\r\nFinancial support by the Polish National Science Center, grant No. DEC-2012/05/B/ST4/00075, is gratefully acknowledged. The structure is available at the PDB, entry 4ZV7.\r\n