X-ray structure of β-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO2 hydration

Satoshi Mitsuhashi, Tsunehiro Mizushima, Eiki Yamashita, Masaki Yamamoto, Takashi Kumasaka, Hideaki Moriyama, Tatzuo Ueki, Shigetoh Miyachi, Tomitake Tsukihara

Research output: Contribution to journalArticle

120 Citations (Scopus)

Abstract

The carbonic anhydrases (CAs) fall into three evolutionarily distinct families designated α-, β-, and γ-CAs based on their primary structure. β-CAs are present in higher plants, algae, and prokaryotes, and are involved in inorganic carbon utilization. Here, we describe the novel x-ray structure of β-CA from the red alga, Porphyridium purpureum, at 2.2-Å resolution using intrinsic zinc multiwavelength anomalous diffraction phasing. The CA monomer is composed of two internally repeating structures, being folded as a pair of fundamentally equivalent motifs of an α/β domain and three projecting α-helices. The motif is obviously distinct from that of either α- or γ-CAs. This homodimeric CA appears like a tetramer with a pseudo 222 symmetry. The active site zinc is coordinated by a Cys-Asp-His-Cys tetrad that is strictly conserved among the β-CAs. No water molecule is found in a zinc-liganding radius, indicating that the zinc-hydroxide mechanism in α- CAs, and possibly in γ-CAs, is not directly applicable to the case in β- CAs. Zinc coordination environments of the CAs provide an interesting example of the convergent evolution of distinct catalytic sites required for the same CO2 hydration reaction.

Original languageEnglish (US)
Pages (from-to)5521-5526
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number8
DOIs
StatePublished - Feb 25 2000

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Porphyridium
Rhodophyta
Carbonic Anhydrases
Algae
Hydration
Catalytic Domain
X-Rays
X rays
Zinc

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

X-ray structure of β-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO2 hydration. / Mitsuhashi, Satoshi; Mizushima, Tsunehiro; Yamashita, Eiki; Yamamoto, Masaki; Kumasaka, Takashi; Moriyama, Hideaki; Ueki, Tatzuo; Miyachi, Shigetoh; Tsukihara, Tomitake.

In: Journal of Biological Chemistry, Vol. 275, No. 8, 25.02.2000, p. 5521-5526.

Research output: Contribution to journalArticle

Mitsuhashi, S, Mizushima, T, Yamashita, E, Yamamoto, M, Kumasaka, T, Moriyama, H, Ueki, T, Miyachi, S & Tsukihara, T 2000, 'X-ray structure of β-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO2 hydration', Journal of Biological Chemistry, vol. 275, no. 8, pp. 5521-5526. https://doi.org/10.1074/jbc.275.8.5521
Mitsuhashi, Satoshi ; Mizushima, Tsunehiro ; Yamashita, Eiki ; Yamamoto, Masaki ; Kumasaka, Takashi ; Moriyama, Hideaki ; Ueki, Tatzuo ; Miyachi, Shigetoh ; Tsukihara, Tomitake. / X-ray structure of β-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO2 hydration. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 8. pp. 5521-5526.
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