Crystallographic study of wild-type carbonic anhydrase αCA1 from Chlamydomonas reinhardtii

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 66; no. 9; pp. 1082 - 1085
• Main Authors: Suzuki, Kaoru, Shimizu, Satoru, Juan, Ella Czarina Magat, Miyamoto, Takahiro, Fang, Zhang, Hoque, Md. Mominul, Sato, Yoshiteru, Tsunoda, Masaru, Sekiguchi, Takeshi, Takénaka, Akio, Yang, Shi-Yuan
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.09.2010
• Subjects: carbonic anhydrases; Carbonic Anhydrases - chemistry; Chlamydomonas reinhardtii; Chlamydomonas reinhardtii - enzymology; Crystallization Communications; Crystallography, X-Ray
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S174430911002823X

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. reinhardtiiαCA1 has been crystallized in space group P65, 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.