Work

Crystallization and preliminary crystallographic analysis of two eukaryotic fructosyl peptide oxidases

Year: 2013

Type: article

Abstract: Fructosyl peptide oxidase (FPOX) catalyses the oxidation of α-glycated dipeptides such as N(α)-(1-deoxy-D-fructos-1-yl)-L-valyl-L-histidine (Fru-ValHis) and is used in the diagnosis of diabetes mellitus. Here, two thermostable mutants of FPOX, CFP-T7 and EFP-T5M, were crystallized by the sitting-drop vapour-diffusion method. The crystal of CFP-T7 belonged to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 110.09, c = 220.48 Å, and that of EFP-T5M belonged to the monoclinic space group P2(1), with unit-cell parameters a = 43.00, b = 230.05, c = 47.27 Å, β = 116.99°. The crystals of CFP-T7 and EFP-T5M diffracted to 1.8 and 1.6 Å resolution, respectively.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309112051445

Authors: Atsushi Ichiyanagi, Kozo Hirokawa, Keiko Gomi, Toru Nakatsu, Hiroaki Kato, Naoki Kajiyama

Institutions: Kikkoman (Japan), Kyoto University

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: Japan Society for the Promotion of Science

Awards: Protein interaction analysis of circadian clock protein, Creation of a high efficient luciferase