1F7K

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

Summary for 1F7K

• Entry DOI: 10.2210/pdb1f7k/pdb
• Related: 1F7D 1F7N 1F7O 1F7P 1F7Q 1F7R
• Descriptor: POL POLYPROTEIN, MAGNESIUM ION, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: eight stranded beta barrel protein, viral protein, hydrolase
• Biological source: Feline immunodeficiency virus
• Total number of polymer chains: 2
• Total formula weight: 30149.62

Authors

Prasad, G.S.,Stura, E.A.,Elder, J.H.,Stout, C.D. (deposition date: 2000-06-27, release date: 2000-09-06, Last modification date: 2024-02-07)

Primary citation

Prasad, G.S.,Stura, E.A.,Elder, J.H.,Stout, C.D.
Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms.
Acta Crystallogr.,Sect.D, 56:1100-1109, 2000

PubMed Abstract: 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.

PubMed: 10957629
DOI: 10.1107/S0907444900009197

Experimental method

X-RAY DIFFRACTION (2.2 Å)