4BLC

THE STRUCTURE OF ORTHORHOMBIC CRYSTALS OF BEEF LIVER CATALASE

4BLC の概要

• エントリーDOI: 10.2210/pdb4blc/pdb
• 分子名称: PROTEIN (CATALASE), PROTOPORPHYRIN IX CONTAINING FE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: lattice contact, heme protein, oxidoreductase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Peroxisome: P00432
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 236105.49

構造登録者

Ko, T.P.,Day, J.,Malkin, A.,McPherson, A. (登録日: 1998-09-27, 公開日: 1998-10-14, 最終更新日: 2023-09-13)

主引用文献

Ko, T.P.,Day, J.,Malkin, A.J.,McPherson, A.
Structure of orthorhombic crystals of beef liver catalase.
Acta Crystallogr.,Sect.D, 55:1383-1394, 1999

PubMed Abstract: The growth mechanisms and physical properties of the orthorhombic crystal form of beef liver catalase were investigated using in situ atomic force microscopy (AFM). It was observed that the crystals grow in the <001> direction by an unusual progression of sequential two-dimensional nuclei of half unit-cell layers corresponding to the 'bottoms' and 'tops' of unit cells. These were easily discriminated by their alternating asymmetric shapes and their strong growth-rate anisotropy. This pattern has not previously been observed with other macromolecular crystals. Orthorhombic beef liver catalase crystals exhibit an extremely high defect density and incorporate great numbers of misoriented microcrystals, revealed intact by etching experiments, which may explain their marginal diffraction properties. To facilitate interpretation of AFM results in terms of intermolecular interactions, the structure of the orthorhombic crystals, having an entire tetramer of the enzyme as the asymmetric unit, was solved by molecular replacement using a model derived from a trigonal crystal form. It was subsequently refined by conventional techniques. Although the packing of molecules in the two unit cells was substantially different, with very few exceptions no significant differences in the molecular structures were observed. In addition, no statistically significant deviation from ideal 222 molecular symmetry appeared within the tetramer. The packing of molecules in the crystal revealed by X-ray analysis explained in a satisfying way the process of crystal growth revealed by AFM.

PubMed: 10417406
DOI: 10.1107/S0907444999007052

実験手法

X-RAY DIFFRACTION (2.3 Å)