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

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• 作者：Zoran &Scaron ; tefani膰^a ; Marta Narczyk^b ; Goran Mikleu&scaron ; evi膰^a ; Beata Wielgus-Kutrowska^b ; Agnieszka Bzowska^b ; ^{abzowska@biogeo.uw.edu.pl} ; Marija Lui膰^a ; ^{marija.luic@irb.hr}
• 关键词：PNP ; purine nucleoside phosphorylase ; FA ; formycin A ; PNP/Pi ; complex of PNP and phosphate ; Kd ; dissociation constant
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：5 April, 2012
• 卷：586
• 期：7
• 页码：967-971
• 文件大小：1313 K

摘要

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 鈥渟tandard鈥?phosphate binding site.

Structured summary of protein interactions

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