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Crystallization and preliminary X‐ray crystallographic analysis of human peptidylarginine deiminase type III
Author(s) -
Unno Masaki,
Kizawa Kenji,
Ishihara Makiko,
Takahara Hidenari
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112015333
Subject(s) - crystallization , arginine deiminase , crystallography , polyethylene glycol , chemistry , molecular replacement , molecule , arginine , citrulline , crystal structure , biochemistry , amino acid , organic chemistry
In the presence of calcium ions, human peptidylarginine deiminase (PAD) converts arginine residues in proteins to citrulline. Of the five known human PAD enzymes, the type III isozyme (PAD3) exhibits the highest specificity for synthetic and natural substrates. This study aimed to determine the structure of PAD3 in order to elucidate its selective citrullination mechanism. Crystals of PAD3 obtained using polyethylene glycol 400 as a precipitant diffracted to 2.95 Å resolution using synchrotron radiation. They belonged to space group R 3, with unit‐cell parameters a = b = 114.97, c = 332.49 Å (hexagonal axes). Assuming two molecules were contained in an asymmetric unit, the calculated Matthews coefficient was 2.83 Å 3  Da −1 , corresponding to a solvent content of 56.6%. Initial phases were determined using PAD4 as a molecular‐replacement model.

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