1DYT

X-ray crystal structure of ECP (RNase 3) at 1.75 A

Summary for 1DYT

• Entry DOI: 10.2210/pdb1dyt/pdb
• Descriptor: EOSINOPHIL CATIONIC PROTEIN, FE (III) ION, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: hydrolase, eosinophil cationic protein, ecp, rnase 3
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasmic granule: P12724
• Total number of polymer chains: 2
• Total formula weight: 32077.94

Authors

Mallorqui-Fernandez, G.,Pous, J.,Peracaula, R.,Maeda, T.,Tada, H.,Yamada, H.,Seno, M.,De Llorens, R.,Gomis-Rueth, F.X.,Coll, M. (deposition date: 2000-02-08, release date: 2001-02-08, Last modification date: 2024-11-06)

Primary citation

Mallorqui-Fernandez, G.,Pous, J.,Peracaula, R.,Maeda, T.,Tada, H.,Yamada, H.,Seno, M.,De Llorens, R.,Gomis-Rueth, F.X.,Coll, M.
Three-Dimensional Crystal Structure of Human Eosinophil Cationic Protein (Rnase 3) at 1.75 A Resolution.
J.Mol.Biol., 300:1297-, 2000

PubMed Abstract: Eosinophil cationic protein (ECP; RNase 3) is a human ribonuclease found only in eosinophil leukocytes that belongs to the RNase A superfamily. This enzyme is bactericidal, helminthotoxic and cytotoxic to mammalian cells and tissues. The protein has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data up to 1. 75 A resolution. The molecule displays the alpha+beta folding topology typical for members of the ribonuclease A superfamily. The catalytic active site residues are conserved with respect to other ribonucleases of the superfamily but some differences appear at substrate recognition subsites, which may account, in part, for the low catalytic activity. Most strikingly, 19 surface-located arginine residues confer a strong basic character to the protein. The high concentration of positive charges and the particular orientation of the side-chains of these residues may also be related to the low activity of ECP as a ribonuclease and provides an explanation for its unique cytotoxic role through cell membrane disruption.

PubMed: 10903870
DOI: 10.1006/JMBI.2000.3939

Experimental method

X-RAY DIFFRACTION (1.75 Å)