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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt 9):1082-5. doi: 10.1107/S174430911002823X. Epub 2010 Aug 28.

Crystallographic study of wild-type carbonic anhydrase alpha CA1 from Chlamydomonas reinhardtii.

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1
College of Science and Engineering, Iwaki-Meisei University, Chuodai-iino, Iwaki, Fukushima 970-8551, Japan.

Abstract

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.

PMID:
20823532
PMCID:
PMC2935233
DOI:
10.1107/S174430911002823X
[Indexed for MEDLINE]
Free PMC Article
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