Acta Crystallographica Section D

Biological Crystallography

Volume 56, Part 2 (February 2000)

short communications

 

Structure of human erythrocyte catalase

T.-P. Ko, M. K. Safo, F. N. Musayev, M. L. Di Salvo, C. Wang, S.-H. Wu and D. J. Abraham

Abstract: Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2₁2₁2₁ and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 Å, was determined and refined with 2.75 Å resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R_free were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.

PDB reference: 1qqw

Keywords: catalase; NADPH.

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