Crystallization and preliminary X-ray analysis of the isomerase domain of glucosamine-6-phosphate synthase from Candida albicans.
Glucosamine-6-phosphate synthase (EC 2.6.1.16) catalyses the first and practically irreversible step in the hexosamine metabolism pathway, the end product of which, uridine 5'-diphospho-N-acetyl D-glucosamine, is an essential substrate for assembly of the cell wall. The isomerase domain, consisting of residues 346-712 (42 kDa), of glucosamine-6-phosphate synthase from Candida albicans has been crystallized. X-ray analysis revealed that the crystals belonged to space group I4, with unit-cell parameters a = b = 149, c = 103 A. Diffraction data were collected to 3.8 A. Preliminary results from molecular replacement using the homologous bacterial monomer reveal that the asymmetric unit contains two monomers that resemble a bacterial dimer. The crystal lattice consists of pairs of such symmetry-related dimers forming elongated tetramers.
Olchowy
Jaroslaw
J
Department of Pharmaceutical Technology and Biochemistry, Gdansk University of Technology, ul. Narutowicza 11/12, 80-952 Gdansk, Poland.
Jedrzejczak
Robert
R
Milewski
Slawomir
S
Rypniewski
Wojciech
W
D019747:Aldose-Ketose Isomerases / Q000737:chemistry; D000946:Antigens, Fungal / Q000737:chemistry; D002176:Candida albicans / Q000201:enzymology*; D002473:Cell Wall; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / Q000737:chemistry*; D007535:Isomerases / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D000946:Antigens, Fungal; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); D007535:Isomerases; D019747:Aldose-Ketose Isomerases