Crystallographic study of wild-type carbonic anhydrase αCA1 from<i>Chlamydomonas reinhardtii</i>

Suzuki, Kaoru; Shimizu, Satoru; Juan, E.C.M.; Miyamoto, Terumasa; Zhang, Fang; Hoque, M.M.; Sato, Yoshihiko; Tsunoda, Masaru; Sekiguchi, Toshio; Takénaka, Akio; Yang, Shuai

doi:10.1107/s174430911002823x

Acta Cryst Sect F

2010

DOI: 10.1107/s174430911002823x

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Crystallographic study of wild-type carbonic anhydrase αCA1 fromChlamydomonas reinhardtii

Kaoru Suzuki

Satoru Shimizu

E.C.M. Juan

et al.

Abstract: Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (CA, CA and CA). Most CA enzymes are monomeric, but CA1 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 CA1 has been cr… Show more

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Cited by 2 publications

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“…While all three CA families contain zinc, they clearly have evolved independently (Hewett-Emmett and Tashian, 1996). Most aCAs are monomeric, although there are notable exceptions (Whittington et al, 2001;Hilvo et al, 2008;Suzuki et al, 2010Suzuki et al, , 2011Cuesta-Seijo et al, 2011). The aCA active site contains a single zinc molecule coordinated by three His residues and a water molecule (Liljas et al, 1972).…”

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The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO₂

et al. 2016

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Carbonic anhydrases (CAs) are zinc metalloenzymes that interconvert CO 2 and HCO 3 2 . In plants, both a-and b-type CAs are present. We hypothesize that cytoplasmic bCAs are required to modulate inorganic carbon forms needed in leaf cells for carbonrequiring reactions such as photosynthesis and amino acid biosynthesis. In this report, we present evidence that bCA2 and bCA4 are the two most abundant cytoplasmic CAs in Arabidopsis (Arabidopsis thaliana) leaves. Previously, bCA4 was reported to be localized to the plasma membrane, but here, we show that two forms of bCA4 are expressed in a tissue-specific manner and that the two proteins encoded by bCA4 localize to two different regions of the cell. Comparing transfer DNA knockout lines with wild-type plants, there was no reduction in the growth rates of the single mutants, bca2 and bca4. However, the growth rate of the double mutant, bca2bca4, was reduced significantly when grown at 200 mL L 21 CO 2 . The reduction in growth of the double mutant was not linked to a reduction in photosynthetic rate. The amino acid content of leaves from the double mutant showed marked reduction in aspartate when compared with the wild type and the single mutants. This suggests the cytoplasmic CAs play an important but not previously appreciated role in amino acid biosynthesis.Carbonic anhydrases (CAs) are zinc metalloenzymes that catalyze the interconversion of CO 2 and HCO 3 2 . Flowering plants possess members of the aCA, bCA, and gCA families. While all three CA families contain zinc, they clearly have evolved independently (Hewett-Emmett and Tashian, 1996). Most aCAs are monomeric, although there are notable exceptions (Whittington et al., 2001;Hilvo et al., 2008;Suzuki et al., 2010Suzuki et al., , 2011Cuesta-Seijo et al., 2011). The aCA active site contains a single zinc molecule coordinated by three His residues and a water molecule (Liljas et al., 1972). bCAs also contain a zinc active site, although the coordinating molecules are two Cys residues, a His, and a water molecule (Bracey et al., 1994). The active unit of the bCA is a dimer where the active site is located at the interface of the two monomers (Kimber and Pai, 2000). In contrast, gCAs are trimers that have their active site zinc ion situated at the interface of two subunits coordinated by His residues from both subunits (Kisker et al., 1996;Iverson et al., 2000).In Arabidopsis (Arabidopsis thaliana), there are three gCA proteins and two g-like proteins that interact to form an extra structure of complex I of the mitochondrial electron transport chain (Perales et al., 2004;Sunderhaus et al., 2006). Although not active in vitro, gCA has been shown to bind inorganic carbon (Martin et al., 2009), affect complex I levels, plant growth, and gas-exchange rates when deleted (Perales et al., 2004;Soto et al., 2015), and cause plant sterility when ectopically overexpressed ). Arabidopsis has eight aCA genes, but only aCA1, aCA2, and aCA3 appear to be expressed in leaf tissue. aCA1 has been reported to be localized to the c...

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The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO₂

et al. 2016

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The unique structure of carbonic anhydrase αCA1 fromChlamydomonas reinhardtii

Suzuki

Yang

Shimizu

et al. 2011

Acta Crystallogr D Biol Crystallogr

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Chlamydomonas reinhardtii α-type carbonic anhydrase (Cr-αCA1) is a dimeric enzyme that catalyses the interconversion of carbon dioxide and carbonic acid. The precursor form of Cr-αCA1 undergoes post-translational cleavage and N-glycosylation. Comparison of the genomic sequences of precursor Cr-αCA1 and other αCAs shows that Cr-αCA1 contains a different N-terminal sequence and two insertion sequences. A 35-residue peptide in one of the insertion sequences is deleted from the precursor during maturation. The crystal structure of the mature form of Cr-αCA1 has been determined at 1.88 Å resolution. Each subunit is cleaved into the long and short peptides, but they are linked together by a disulfide bond. The two subunits are linked by a disulfide bond. N-Glycosylations occur at three asparagine residues and the attached N-glycans protrude into solvent regions. The subunits consist of a core β-sheet structure composed of nine β-strands. At the centre of the β-sheet is the catalytic site, which contains a Zn atom bound to three histidine residues. The amino-acid residues around the Zn atom are highly conserved in other monomeric and dimeric αCAs. The short peptide runs near the active site and forms a hydrogen bond to the zinc-coordinated residue in the long chain, suggesting an important role for the short peptide in Cr-αCA1 activity.

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Crystallographic study of wild-type carbonic anhydrase αCA1 fromChlamydomonas reinhardtii

Cited by 2 publications

References 34 publications

The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO₂

The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO₂

The unique structure of carbonic anhydrase αCA1 fromChlamydomonas reinhardtii

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Crystallographic study of wild-type carbonic anhydrase αCA1 fromChlamydomonas reinhardtii

Cited by 2 publications

References 34 publications

The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO2

The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO2

The unique structure of carbonic anhydrase αCA1 fromChlamydomonas reinhardtii

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The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO₂

The Cytoplasmic Carbonic Anhydrases βCA2 and βCA4 Are Required for Optimal Plant Growth at Low CO₂