Crystallographic study of wild-type carbonic anhydrase alpha CA1 from Chlamydomonas reinhardtii.
Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (alphaCA, betaCA and gammaCA). Most alphaCA enzymes are monomeric, but alphaCA1 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 alphaCA1 has been crystallized in space group P6(5), with unit-cell parameters a=b=134.3, c=120.2 A. The crystal diffracted to 1.88 A resolution and a preliminary solution of its crystal structure has been obtained by the MAD method.
Suzuki
Kaoru
K
College of Science and Engineering, Iwaki-Meisei University, Chuodai-iino, Iwaki, Fukushima 970-8551, Japan.
Shimizu
Satoru
S
Juan
Ella Czarina Magat
EC
Miyamoto
Takahiro
T
Fang
Zhang
Z
Hoque
Md Mominul
MM
Sato
Yoshiteru
Y
Tsunoda
Masaru
M
Sekiguchi
Takeshi
T
Takénaka
Akio
A
Yang
Shi Yuan
SY
D002256:Carbonic Anhydrases / Q000737:chemistry*; D016825:Chlamydomonas reinhardtii / Q000201:enzymology*; D018360:Crystallography, X-Ray
D002256:Carbonic Anhydrases
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