Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 68, Issue -, Pages 668-670Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309112015333
Keywords
peptidylarginine deiminase III; citrullination; protein-modifying enzymes; dimers
Funding
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) [23121504]
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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 angstrom resolution using synchrotron radiation. They belonged to space group R3, with unit-cell parameters a = b = 114.97, c = 332.49 angstrom (hexagonal axes). Assuming two molecules were contained in an asymmetric unit, the calculated Matthews coefficient was 2.83 angstrom 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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