Crystallization and preliminary X-ray crystallographic studies of Escherichia colixanthine phosphoribosyltransferase

No Thumbnail Available
File version
Author(s)
Vos, S
deJersey, J
Martin, JL
Griffith University Author(s)
Primary Supervisor
Other Supervisors
Editor(s)
Date
1996
Size
File type(s)
Location
License
Abstract

Xanthine phosphoribosyltransferase (XPRT; EC 2.4.2.22) fromEscherichia coliis a purine salvage enzyme which synthesizes the nucleotides GMP, XMP, and IMP. A mutant C59A, which is more stable than wild-type XPRT while retaining high activity, has been prepared and crystallized to give three different crystal forms (A, B, and C). Form A crystals are orthorhombic (P21212), with unit cell dimensionsa= 59.2 Å,b= 92.9 Å,c= 53.2 Å. Form B crystals are monoclinic (C2) with unit cell dimensionsa= 84.4 Å,b= 70.8 Å,c= 54.1 Å, and β = 113.4°, and form C crystals are tetragonal (P41212 or P43212) with unit cell dimensionsa,b= 94 Å,c= 167.5 Å. Wild-type XPRT and a selenomethionine derivative of C59A XPRT have also been crystallized in the orthorhombic form. The selenomethionine derivative was prepared by expressing XPRT in the usualE. colistrain without the need for a methionine auxotroph. Cells were grown in a methionine-deficient medium supplemented with selenomethionine which gave >95% incorporation. Both the wild-type and selenomethionine C59A XPRT crystals are isomorphous with C59A form A crystals.

Journal Title

Journal of Structural Biology

Conference Title
Book Title
Edition
Volume

116

Issue

2

Thesis Type
Degree Program
School
Publisher link
Patent number
Funder(s)
Grant identifier(s)
Rights Statement
Rights Statement
Item Access Status
Note
Access the data
Related item(s)
Subject

Biochemistry and cell biology

Biochemistry and cell biology not elsewhere classified

Zoology

Persistent link to this record
Citation
Collections