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Crystallization and preliminary X-ray diffraction analysis of maize aldose reductase.

ABSTRACT: Maize aldose reductase (AR) is a member of the aldo-keto reductase superfamily. In contrast to human AR, maize AR seems to prefer the conversion of sorbitol into glucose. The apoenzyme was crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 47.2, b = 54.5, c = 100.6 A and one molecule in the asymmetric unit. Synchrotron X-ray diffraction data were collected and a final resolution limit of 2.0 A was obtained after data reduction. Phasing was carried out by an automated molecular-replacement procedure and structural refinement is currently in progress. The refined structure is expected to shed light on the functional/enzymatic mechanism and the unusual activities of maize AR.

SUBMITTER: Kiyota E

PROVIDER: S-EPMC2339750 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of maize aldose reductase.

Kiyota Eduardo E de Sousa Sylvia Morais SM Dos Santos Marcelo Leite ML da Costa Lima Aline A Menossi Marcelo M Yunes José Andrés JA Aparicio Ricardo R

Acta crystallographica. Section F, Structural biology and crystallization communications 20071026 Pt 11

Maize aldose reductase (AR) is a member of the aldo-keto reductase superfamily. In contrast to human AR, maize AR seems to prefer the conversion of sorbitol into glucose. The apoenzyme was crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 47.2, b = 54.5, c = 100.6 A and one molecule in the asymmetric unit. Synchrotron X-ray diffraction data were collected and a final resolution limit of 2.0 A was obtained after data reduction. Phasing was carried out by an automated molecu ...[more]

PMID: 18007059

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