1f7k

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1f7k, resolution 2.20Å

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CRYSTAL STRUCTURES OF FELINE IMMUNODEFICIENCY VIRUS DUTP PYROPHOSPHATASE AND ITS NUCLEOTIDE COMPLEXES IN THREE CRYSTAL FORMS.

Overview

dUTP pyrophosphatase (dUTPase) cleaves the alpha-beta phosphodiester of, dUTP to form pyrophosphate and dUMP, preventing incorporation of uracil, into DNA and providing the substrate for thymine synthesis. Seven crystal, structures of feline immunodeficiency virus (FIV) dUTPase in three crystal, forms have been determined, including complexes with substrate (dUTP), product (dUMP) or inhibitor (dUDP) bound. The native enzyme has been, refined at 1.40 A resolution in a hexagonal crystal form and at 2.3 A, resolution in an orthorhombic crystal form. In the dUDP complex in a cubic, crystal form refined at 2.5 A resolution, the C-terminal conserved P-loop, motif is fully ordered. The analysis defines the roles of five sequence, motifs in interaction with uracil, deoxyribose and the alpha-, beta- and, gamma-phosphates. The enzyme utilizes adaptive recognition to bind the, alpha- and beta-phosphates. In particular, the alpha-beta phosphodiester, adopts an unfavorable eclipsed conformation in the presence of the P-loop., This conformation may be relevant to the mechanism of alpha-beta, phosphodiester bond cleavage.

About this Structure

1F7K is a Single protein structure of sequence from Feline immunodeficiency virus with MG and UMP as ligands. Active as dUTP diphosphatase, with EC number 3.6.1.23 Full crystallographic information is available from OCA.

Reference

Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms., Prasad GS, Stura EA, Elder JH, Stout CD, Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1100-9. PMID:10957629

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