Structure of the T109S mutant of Escherichia coli dihydroorotase complexed with the inhibitor 5-­fluoroorotate: catalytic activity is reflected by the crystal form

Lee, M.; Maher, M.J.; Guss, J.M.

doi:10.1107/S1744309107004009

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 6
DHOase crystal packing. (a, b) Tetragonal FOA complex of T109S DHOase. The monomer in the asymmetric unit is shown in yellow, with the flexible surface loops (residues 105–115) in magenta. The other monomer of the dimer is shown in blue. Other symmetry-related dimers are shown in green. (c, d) Crystal packing of the orthorhombic wild-type DHOase. Chain A with the `loop-out' conformation is shown in yellow and chain B with the `loop-in' conformation in blue. The projection is down along the c axis in (a) and (c) and perpendicular to the c axis in (b) and (d).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 63| Part 3| March 2007| Pages 154-161

https://doi.org/10.1107/S1744309107004009

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