NDLI: Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type III.

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Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type III.

Content Provider	Europe PMC
Author	Unno, Masaki Kizawa, Kenji Ishihara, Makiko Takahara, Hidenari
Copyright Year	2012
Description	Human peptidylarginine deiminase type III was crystallized using polyethylene glycol monomethylether or polyethylene glycol as a precipitant. The crystals belonged to space group R3, with unit-cell parameters a = b = 114.97, c = 332.49 Å (hexagonal axes), and contained two molecules in an asymmetric unit. 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 R3, 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 Å3 Da−1, corresponding to a solvent content of 56.6%. Initial phases were determined using PAD4 as a molecular-replacement model.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC3370906&blobtype=pdf
Volume Number	68
PubMed Central reference number	PMC3370906
Issue Number	Pt 6
Issue Number	pt 6
PubMed reference number	22684066
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications [Acta Crystallogr Sect F Struct Biol Cryst Commun]
e-ISSN	17443091
DOI	10.1107/s1744309112015333
Language	English
Publisher	International Union of Crystallography
Publisher Date	2012-05-23
Access Restriction	Open
Rights License	© International Union of Crystallography 2012
Subject Keyword	peptidylarginine deiminase III citrullination protein-modifying enzymes dimers
Content Type	Text
Resource Type	Article
Subject	Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology

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