Crystallographic study of wild-type carbonic anhydrase aCA1 from Chlamydomonas reinhardtii

Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (aCA, bCA and gCA). Most aCA enzymes are monomeric, but aCA1 from Chlamydomonas reinhardtii is a dimer that is uniquely stabilized by disulfide bonds. In addition, during maturation an...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-09, Vol.66 (9), p.1082-1085
Main Authors: Suzuki, Kaoru, Shimizu, Satoru, Juan, Ella Czarina Magat, Miyamoto, Takahiro, Fang, Zhang, Hoque, MdMominul, Sato, Yoshiteru, Tsunoda, Masaru, Sekiguchi, Takeshi, Takenaka, Akio, Yang, Shi-Yuan
Format: Article
Language:English
Subjects:
Chlamydomonas reinhardtii
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Summary:Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (aCA, bCA and gCA). Most aCA enzymes are monomeric, but aCA1 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 aCA1 has been crystallized in space group P65, with unit-cell parameters a = b = 134.3, c = 120.2 Aa. The crystal diffracted to 1.88 Aa resolution and a preliminary solution of its crystal structure has been obtained by the MAD method.
ISSN:1744-3091
1744-3091
DOI:10.1107/S174430911002823X