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. 2000 Jul;1(1):16-7.
doi: 10.1093/embo-reports/kvd016.

A wheel invented three times. The molecular structures of the three carbonic anhydrases

A Liljas  1 , M Laurberg
Affiliations

A wheel invented three times. The molecular structures of the three carbonic anhydrases

A Liljas et al. EMBO Rep. 2000 Jul.
No abstract available

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Figures

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Fig. 1. The tertiary structures of the three forms of carbonic anhydrase. From top to bottom: α-CA monomer; algal β-CA dimer with internal repeat [the unique (monomer) fold is highlighted]; pea β-CA octamer; γ-CA trimer. For the oligomeric forms of the enzyme, one monomer is highlighted with the β-strands in yellow and the α-helices in blue. The other monomers are in light gray. The zinc ions are indicated by red spheres.
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Fig. 2. Schematic representations of the active sites of the three forms of carbonic anhydrase with a bound bicarbonate ion (α-CA, Liljas et al., 1994; β-CA, Protein Data Bank entry 1QRL). The location of HCO3 in the active site of γ-CA is tentative and made in analogy to the situation in the other two forms. The proximity of an obligate hydrogen bond acceptor close to the free ligand position at the zinc ion (red sphere) seems in all cases to dictate the ion’s orientation. Thus, the catalytic mechanism is likely to be the same.
See this image and copyright information in PMC

References

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