Open AccessCrystallographic study of wild‐type carbonic anhydrase αCA1 from Chlamydomonas reinhardtii
Author(s) -
Suzuki Kaoru,
Shimizu Satoru,
Juan Ella Czarina Magat,
Miyamoto Takahiro,
Fang Zhang,
Hoque Md. Mominul,
Sato Yoshiteru,
Tsunoda Masaru,
Sekiguchi Takeshi,
Takénaka Akio,
Yang ShiYuan
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911002823x
Subject(s) - chlamydomonas reinhardtii , carbonic anhydrase , dimer , chemistry , monomer , crystallography , asparagine , crystal structure , enzyme , stereochemistry , biochemistry , gene , organic chemistry , mutant , polymer
Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (αCA, βCA and γCA). Most αCA enzymes are monomeric, but αCA1 from Chlamydomonas reinhardtii is a dimer that is uniquely stabilized by disulfide bonds. In addition, during maturation an internal peptide of 35 residues is removed and three asparagine residues are glycosylated. In order to obtain insight into the effects of these structural features on CA function, wild‐type C. reinhardtii αCA1 has been crystallized in space group P 6 5 , with unit‐cell parameters a = b = 134.3, c = 120.2 Å. The crystal diffracted to 1.88 Å resolution and a preliminary solution of its crystal structure has been obtained by the MAD method.