7C5X

Crystal structure of the iota-carbonic anhydrase from eukaryotic microalga complexed with bicarbonate

Summary for 7C5X

• Entry DOI: 10.2210/pdb7c5x/pdb
• Descriptor: iota-carbonic anhydrase, BICARBONATE ION (3 entities in total)
• Functional Keywords: carbonic anhydrase, bicarbonate complex, lyase
• Biological source: Bigelowiella natans
• Total number of polymer chains: 2
• Total formula weight: 111214.37

Authors

Senda, M.,Senda, T. (deposition date: 2020-05-20, release date: 2021-04-28, Last modification date: 2023-11-29)

Primary citation

Hirakawa, Y.,Senda, M.,Fukuda, K.,Yu, H.Y.,Ishida, M.,Taira, M.,Kinbara, K.,Senda, T.
Characterization of a novel type of carbonic anhydrase that acts without metal cofactors.
Bmc Biol., 19:105-105, 2021

PubMed Abstract: Carbonic anhydrases (CAs) are universal metalloenzymes that catalyze the reversible conversion of carbon dioxide (CO) and bicarbonate (HCO). They are involved in various biological processes, including pH control, respiration, and photosynthesis. To date, eight evolutionarily unrelated classes of CA families (α, β, γ, δ, ζ, η, θ, and ι) have been identified. All are characterized by an active site accommodating the binding of a metal cofactor, which is assumed to play a central role in catalysis. This feature is thought to be the result of convergent evolution.

PubMed: 34006275
DOI: 10.1186/s12915-021-01039-8

Experimental method

X-RAY DIFFRACTION (2.55 Å)