1f4j
STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE
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OverviewOverview
The structure of catalase from human erythrocytes (HEC) was determined in, tetragonal crystals of space group I4(1) by molecular-replacement methods, using the orthorhombic crystal structure as a search model. It was then, refined in a unit cell of dimensions a = b = 203.6 and c = 144.6 A, yielding R and R(free) of 0.196 and 0.244, respectively, for all data at, 2.4 A resolution. A major difference of the HEC structure in the, tetragonal crystal compared with the orthorhombic structure was the, omission of a 20-residue N-terminal segment corresponding to the first, exon of the human catalase gene. The overall structures were otherwise, identical in both crystal forms. The NADPH-binding sites were empty in all, four subunits and bound water molecules were observed at the active sites., The structure of the C-terminal segment, which corresponds to the last, exon, remained undetermined. The tetragonal crystals showed a, pseudo-4(1)22 symmetry in molecular packing. Two similar types of lattice, contact interfaces between the HEC tetramers were observed; they were, related by the pseudo-dyad axes.
DiseaseDisease
Known disease associated with this structure: Acatalasemia OMIM:[115500]
About this StructureAbout this Structure
1F4J is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Catalase, with EC number 1.11.1.6 Full crystallographic information is available from OCA.
ReferenceReference
Structure of tetragonal crystals of human erythrocyte catalase., Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. PMID:11134921
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