3boc

Carbonic anhydrase from marine diatom Thalassiosira weissflogii- zinc bound domain 2 (CDCA1-R2)

spinqualitylabelsall models 3boc, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3boc is a 1 chain structure with sequence from Thalassiosira weissflogii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 3bob Gene: cdca1 (Thalassiosira weissflogii) Activity: Carbonate dehydratase, with EC number 4.2.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Carbonic anhydrase, a zinc enzyme found in organisms from all kingdoms, catalyses the reversible hydration of carbon dioxide and is used for inorganic carbon acquisition by phytoplankton. In the oceans, where zinc is nearly depleted, diatoms use cadmium as a catalytic metal atom in cadmium carbonic anhydrase (CDCA). Here we report the crystal structures of CDCA in four distinct forms: cadmium-bound, zinc-bound, metal-free and acetate-bound. Despite lack of sequence homology, CDCA is a structural mimic of a functional beta-carbonic anhydrase dimer, with striking similarity in the spatial organization of the active site residues. CDCA readily exchanges cadmium and zinc at its active site--an apparently unique adaptation to oceanic life that is explained by a stable opening of the metal coordinating site in the absence of metal. Given the central role of diatoms in exporting carbon to the deep sea, their use of cadmium in an enzyme critical for carbon acquisition establishes a remarkable link between the global cycles of cadmium and carbon. Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms.,Xu Y, Feng L, Jeffrey PD, Shi Y, Morel FM Nature. 2008 Mar 6;452(7183):56-61. PMID:18322527 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carbonic anhydrase

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