XRD1 Highlights

Stereoview of the electron density map and corresponding models of HCAII active site in complex with (a) CO₂ at 1.56 A resolution and (b) HCO₃^- at 1.66 A resolution. The bicarbonate has van der Walls contacts with the same residues as CO₂.

Carbonic anhydrase, a zinc metalloenzyme, catalyzes the reversible hydration of carbon dioxide to bicarbonate. It is involved in processes connected with acid–base homeostasis, respiration, and photosynthesis. More than 100 distinct human carbonic anhydrase II (HCAII) 3D structures have been generated in last 3 decades [Liljas A, et al. (1972) Nat New Biol 235:131–137], but a structure of an HCAII in complex with CO₂ or HCO₃⁻ has remained elusive.
Here, we report previously undescribed structures of

Retieve Article

Structural study of X-ray induced activation of carbonic anhydrase; Sjöblom B., Polentarutti M. and Djinović-Carugo K., PNAS 106, 10609 (2009); doi:10.1073/pnas.0904184106