3boj: Difference between revisions

Revision as of 17:01, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3boj.png

Template:STRUCTURE 3boj

Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 1 without bound metal (CDCA1-R1)Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 1 without bound metal (CDCA1-R1)

Template:ABSTRACT PUBMED 18322527

About this StructureAbout this Structure

3BOJ is a Single protein structure of sequence from Thalassiosira weissflogii. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Sun Jul 27 17:01:52 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 1 without bound metal (CDCA1-R1)'''
+===Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 1 without bound metal (CDCA1-R1)===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18322527}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_18322527}}
 ==About this Structure==
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 [[Category: Marine diatom]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:57:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:01:52 2008''