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Crystallization and preliminary X-ray analysis of the isomerase domain of glucosamine-6-phosphate synthase from Candida albicans.

ABSTRACT: 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.

SUBMITTER: Olchowy J 

PROVIDER: S-EPMC1978140 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of the isomerase domain of glucosamine-6-phosphate synthase from Candida albicans.

Olchowy Jaroslaw J   Jedrzejczak Robert R   Milewski Slawomir S   Rypniewski Wojciech W  

Acta crystallographica. Section F, Structural biology and crystallization communications 20051020 Pt 11

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 para  ...[more]

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