Preliminary crystallographic analysis of 4-oxalocrotonate tautomerase reveals the oligomeric structure of the enzyme.
Crystals of recombinant 4-oxalocrotonate tautomerase from Pseudomonas sp. strain CF600 have been obtained in a form suitable for X-ray analysis. The enzyme is a highly efficient catalyst and is unusual in that it consists of subunits of only 62 amino acids. It crystallises in the triclinic space group, P1, with unit cell dimensions a = 39.6 A, b = 51.5 A, c = 51.6 A, alpha = 60.0 degrees, beta = 81.4 degrees, gamma = 69.6 degrees. The crystals diffract to beyond 1.9 A resolution and are stable to irradiation with X-rays. Preliminary crystallographic data are not consistent with the previously suggested pentameric structure, but indicate that the complex is in fact a hexamer with 32 symmetry.
Department of Chemistry, University of York, Heslington, U.K.
D I
DI
Roper
H S
HS
Subramanya
V
V
Shingler
D B
DB
Wigley
D003198:Computer Simulation; D018360:Crystallography, X-Ray; D007535:Isomerases / Q000737:chemistry*; D008958:Models, Molecular; D008970:Molecular Weight; D010984:Platinum / Q000737:chemistry; D011108:Polymers; D011549:Pseudomonas / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D012015:Reference Standards
D011108:Polymers; D011994:Recombinant Proteins; D010984:Platinum; C021918:4-oxalocrotonate tautomerase; D007535:Isomerases