7bf0

Zn-bound domain 3 of CDCA1 in complex with carbon dioxide

spinqualitylabelsall models 7bf0, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bf0 is a 2 chain structure with sequence from Conticribra weissflogii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CL, CO2, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q50EL4_THAWE Publication Abstract from PubMed CDCA1 is a very peculiar member of the Carbonic Anhydrase (CA) family. It has been the first enzyme to show an efficient utilization of Cd(II) ions in Nature and a unique adaptation capability to live on the surface ocean. Indeed, in this environment, which is extremely depleted in essential metal ions, CDCA1 can utilize Zn(II) or Cd(II) as catalytic metal to support the metabolic needs of fast growing diatoms. In this paper we demonstrate a further catalytic versatility of this enzyme by using a combination of X-ray crystallography, molecular dynamics simulations and enzymatic experiments. First we identified the CO2 binding site and the way in which this substrate travels from the environment to the enzyme active site. Then, starting from the observation of a structural similarity with the substrate entry route of CS2 hydrolase from Acidanius A1-3, we hypothesized and demonstrated that also CS2 is a substrate for CDCA1. This finding is new and unexpected since until now only few CS2 hydrolases have been characterized, and none of them is reported to have any CO2 hydratase action. The physiological implications of this supplementary catalytic activity still remain to be unveiled. We suggest here that it could represent another ability of diatoms expressing CDCA1 to adapt to the external environment. Indeed, the ability of this enzyme to convert CS2 could represent an alternative source of carbon acquisition for diatoms, in addition to CO2. Zeta-carbonic anhydrases show CS2 hydrolase activity: A new metabolic carbon acquisition pathway in diatoms?,Alterio V, Langella E, Buonanno M, Esposito D, Nocentini A, Berrino E, Bua S, Polentarutti M, Supuran CT, Monti SM, De Simone G Comput Struct Biotechnol J. 2021 Jun 5;19:3427-3436. doi:, 10.1016/j.csbj.2021.05.057. eCollection 2021. PMID:34194668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carbonic anhydrase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA