Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?
Marija Luić
; Division of Physical Chemistry, Ruđer Bošković Institute, POB 180, HR-10002 Zagreb, Croatia
Zoran Štefanić
; Division of Physical Chemistry, Ruđer Bošković Institute, POB 180, HR-10002 Zagreb, Croatia
APA 6th Edition Luić, M. i Štefanić, Z. (2016). Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?. Croatica Chemica Acta, 89 (2), 197-202. https://doi.org/10.5562/cca2872
MLA 8th Edition Luić, Marija i Zoran Štefanić. "Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?." Croatica Chemica Acta, vol. 89, br. 2, 2016, str. 197-202. https://doi.org/10.5562/cca2872. Citirano 09.03.2021.
Chicago 17th Edition Luić, Marija i Zoran Štefanić. "Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?." Croatica Chemica Acta 89, br. 2 (2016): 197-202. https://doi.org/10.5562/cca2872
Harvard Luić, M., i Štefanić, Z. (2016). 'Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?', Croatica Chemica Acta, 89(2), str. 197-202. https://doi.org/10.5562/cca2872
Vancouver Luić M, Štefanić Z. Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?. Croatica Chemica Acta [Internet]. 2016 [pristupljeno 09.03.2021.];89(2):197-202. https://doi.org/10.5562/cca2872
IEEE M. Luić i Z. Štefanić, "Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?", Croatica Chemica Acta, vol.89, br. 2, str. 197-202, 2016. [Online]. https://doi.org/10.5562/cca2872
Sažetak It is generaly believed that enzymes retain most of their functionality in the crystal form due to the large solvent content of protein crystals. This is facilitated by the fact that their natural environment in solution is not too far from the one found in the crystal form. Nevertheless, if the nature of the enzyme is such to require conformational changes, overcoming of the crystal packing constraints may prove to be too difficult. Such conformational change is present in one class of enzymes (purine nucleoside phosphorylases), that is the subject of our scientific interest for many years. The influence of crystal symmetry and crystal packing on the conformation of the active sites in the case of homohexameric purine nucleoside phosphorylases is presented and analysed.