Crystallographic study of wild-type carbonic anhydrase αCA1 from Chlamydomonas reinhardtii
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...
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| Published in | Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 66; no. 9; pp. 1082 - 1085 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
International Union of Crystallography
01.09.2010
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| Abstract | 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. |
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| AbstractList | 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. 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. 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. reinhardtii αCA1 has been crystallized in space group P 6 5 , 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. The carbonic anhydrase αCA1 from C. reinhardtii is a dimeric class αCA enzyme with post-translational glycosylation at three asparagine residues and proteolytic removal of a short peptide. The mature enzyme has been crystallized, MAD data have been collected to 1.88 Å resolution and a preliminary solution of the crystal structure has been obtained. 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. reinhardtii αCA1 has been crystallized in space group P 6 5 , 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. |
| Author | Tsunoda, Masaru Miyamoto, Takahiro Juan, Ella Czarina Magat Suzuki, Kaoru Shimizu, Satoru Yang, Shi-Yuan Takénaka, Akio Hoque, Md. Mominul Fang, Zhang Sato, Yoshiteru Sekiguchi, Takeshi |
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| Snippet | Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (αCA, βCA and γCA). Most αCA enzymes are... Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (alphaCA, betaCA and gammaCA). Most alphaCA... The carbonic anhydrase αCA1 from C. reinhardtii is a dimeric class αCA enzyme with post-translational glycosylation at three asparagine residues and... |
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| SubjectTerms | carbonic anhydrases Carbonic Anhydrases - chemistry Chlamydomonas reinhardtii Chlamydomonas reinhardtii - enzymology Crystallization Communications Crystallography, X-Ray |
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| Title | Crystallographic study of wild-type carbonic anhydrase αCA1 from Chlamydomonas reinhardtii |
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