Preliminary crystallographic study of protocatechuate 3,4-dioxygenase from Brevibacterium fuscum.
The enzyme protocatechuate 3,4-dioxygenase from the Gram positive organism Brevibacterium fuscum crystallizes in the triclinic space group P1 with unit cell dimensions a = 96.1 A, b = 97.2 A, c = 118.1 A and alpha = 113.9 degrees, beta = 90.7 degrees, gamma = 117.8 degrees. The rod-like crystals diffract to 2.4 A resolution. Rotation function analysis suggests that there are six promoters arranged with local 32 symmetry in the asymmetric unit rather than the previously proposed pentameric complex.
Earhart
C A
CA
Department of Biochemistry, University of Minnesota Medical School, Minneapolis 55455.
Radhakrishnan
R
R
Orville
A M
AM
Lipscomb
J D
JD
Ohlendorf
D H
DH
D001951:Brevibacterium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D011487:Protein Conformation; D011520:Protocatechuate-3,4-Dioxygenase / Q000737:chemistry* / Q000302:isolation & purification
D011520:Protocatechuate-3,4-Dioxygenase