New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A

Crosbi ID183136
Bib IRB ID575760
Year2012
StatusObjavljeno
Typeprilog u časopisu
Subtypeizvorni znanstveni rad
AuthorsŠtefanić, Zoran ; Narczyk, Marta ; Mikleušević, Goran ; Wielgus-Kutrowska, Beata ; Bzowska, Agnieszka ; Luić, Marija
JournalFEBS letters
Volume586
Issue7
Pagesstr. 967-971
DOI10.1016/j.febslet.2012.02.039
ISSN0014-5793
EISSN1873-3468
Titles

en original New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A

Abstracts
en original

Purine nucleoside phosphorylase (PNP) from Escherichia coli is a homohexamer that catalyses the phosphorolytic cleavage of the glycosidic bond of purine nucleosides. The first crystal structure of the ternary complex of this enzyme (with a phosphate ion and formycin A), which is biased by neither the presence of an inhibitor nor sulfate as a precipitant, is presented. The structure reveals, in some active sites, an unexpected and never before observed binding site for phosphate and exhibits a stoichiometry of two phosphate molecules per enzyme subunit. Moreover, in these active sites, the phosphate and nucleoside molecules are found not to be in direct contact. Rather, they are bridged by three water molecules that occupy the “standard” phosphate binding site.

Keywords

en original Purine nucleoside phosphorylase ; Formycin ; Crystal structure ; Fluorescence titration ; Binding site ; Stoichiometrypurine nucleoside phosphorylase ; formycin ; crystal structure ; fluorescence titration ; binding site ; stoichiometry

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Citations
Štefanić, Zoran ; Narczyk, Marta ; Mikleušević, Goran ; Wielgus-Kutrowska, Beata ; Bzowska, Agnieszka ; Luić, Marija
New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A // FEBS letters, 586 (2012), 7; 967-971. doi: 10.1016/j.febslet.2012.02.039
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