| Literature DB >> 20823532 |
Kaoru Suzuki1, Satoru Shimizu, Ella Czarina Magat Juan, Takahiro Miyamoto, Zhang Fang, Md Mominul Hoque, Yoshiteru Sato, Masaru Tsunoda, Takeshi Sekiguchi, Akio Takénaka, Shi Yuan Yang.
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.Entities:
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Year: 2010 PMID： 20823532 PMCID： PMC2935233 DOI： 10.1107/S174430911002823X
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091