Open AccessCrystallization and preliminary X‐ray analysis of the isomerase domain of glucosamine‐6‐phosphate synthase from Candida albicans
Author(s) -
Olchowy Jaroslaw,
Jedrzejczak Robert,
Milewski Slawomir,
Rypniewski Wojciech
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910503318x
Subject(s) - dimer , atp synthase , isomerase , glucosamine , monomer , chemistry , candida albicans , crystallography , stereochemistry , molecular replacement , enzyme , crystallization , biochemistry , crystal structure , biology , organic chemistry , microbiology and biotechnology , polymer
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 I 4, with unit‐cell parameters a = b = 149, c = 103 Å. Diffraction data were collected to 3.8 Å. 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.