Pregled bibliografske jedinice broj: 846564
Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?
Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases? // Croatica chemica acta, 89 (2016), 2; 197-202 doi:10.5562/cca2872 (međunarodna recenzija, članak, znanstveni)
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Naslov
Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?
Autori
Luić, Marija ; Štefanić, Zoran
Izvornik
Croatica chemica acta (0011-1643) 89
(2016), 2;
197-202
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
crystal symmetry ; crystal packing ; active site conformation ; enzyme reaction ; purine nucleoside phosphorylase
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.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija, Računarstvo
POVEZANOST RADA
Projekti:
HRZZ-IP-2013-11-7423 - Enzimi purinskog reciklirajućeg ciklusa iz Helicobacter pylori i Escherichie coli (PSPE) (Luić, Marija, HRZZ - 2013-11) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
