Crystallization and preliminary X-ray analysis of chondroitin sulfate ABC lyases I and II from Proteus vulgaris.
Chondroitin sulfate ABC lyases (E.C. 4.2.2.4) are broad-specificity glycosaminoglycan-degrading enzymes. Their preferred substrates are chondroitin sulfate and dermatan sulfate, which are broken down to short oligosaccharides. Proteus vulgaris produces two such lyases, ABC lyase I and II, with molecular weights of 112-113 kDa. Diffraction-quality crystals of both enzymes have been obtained by the hanging-drop vapour-diffusion method. ABC lyase I crystallizes in space group P2(1)2(1)2(1), with unit-cell parameters a = 49.3, b = 95.1, c = 230.0 A, Z = 4, and diffracts to 1.9 A resolution. Crystals of ABC lyase II belong to space group P1, with unit-cell parameters a = 64.2, b = 64.3, c = 142.1 A, alpha = 95.7, beta = 98. 1, gamma = 95.5 degrees, Z = 2; diffraction extends to at least 2.1 A.
Huang
W
W
Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec, H4P 2R2, Canada, and Montreal Joint Centre for Structural Biology, Canada.
Matte
A
A
Suzuki
S
S
Sugiura
N
N
Miyazono
H
H
Cygler
M
M
D019765:Chondroitin ABC Lyase / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D007527:Isoenzymes / Q000737:chemistry*; D011487:Protein Conformation; D011514:Proteus vulgaris / Q000201:enzymology*
D007527:Isoenzymes; D019765:Chondroitin ABC Lyase