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Oligomeric Symmetry of Purine Nucleoside Phosphorylases

Gomaz, Boris; Štefanić, Zoran (2024) Oligomeric Symmetry of Purine Nucleoside Phosphorylases. Symmetry, 16 (1). ISSN 2073-8994

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Many enzymes are composed of several identical subunits, which are arranged in a regular fashion and usually comply with some definite symmetry. This symmetry may be approximate or exact and may or may not coincide with the symmetry of crystallographic packing. Purine nucleoside phosphorylases (PNP) are a class of oligomeric enzymes that show an interesting interplay between their internal symmetry and the symmetry of their crystal packings. There are two main classes of this enzyme: trimeric PNPs, or “low-molecular-mass” proteins, which are found mostly in eukaryotic organisms, and hexameric PNPs, or “high-molecular-mass” proteins, which are found mostly in prokaryotic organisms. Interestingly, these two enzyme classes share only 20–30% sequence identity, but the overall fold of the single monomer is similar, yet this monomeric building block results in a different quaternary structure. To investigate this interplay of symmetry in this class of enzymes, a comprehensive database of all PNPs is constructed, containing their local symmetries and interface information.

Item Type: Article
Uncontrolled Keywords: oligomeric enzymes; purine nucleoside phosphorylases; crystal symmetry
Subjects: NATURAL SCIENCES > Chemistry
Divisions: Division of Physical Chemistry
Project titleProject leaderProject codeProject type
Alosterički komunikacijski putevi u oligomernim enzimima-ALOKOMP/ALOCOMPZoran Štefanić; Marko Tomin; Aleksandra Maršavelski; Alessandro Pandini; Bojana Dalbelo-Bašić; Agnieszka BzowskaIP-2019-04-6764HRZZ
Depositing User: Zoran Štefanić
Date Deposited: 06 Feb 2024 15:14
DOI: 10.3390/sym16010124

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