3bob
From Proteopedia
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- | [[Image:3bob.jpg|left|200px]] | + | [[Image:3bob.jpg|left|200px]] |
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- | '''Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 2''' | + | {{Structure |
+ | |PDB= 3bob |SIZE=350|CAPTION= <scene name='initialview01'>3bob</scene>, resolution 1.45Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Cd+Binding+Site+For+Residue+A+1001'>AC1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= cdca1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67004 Thalassiosira weissflogii]) | ||
+ | }} | ||
+ | |||
+ | '''Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 2''' | ||
+ | |||
+ | |||
+ | ==Overview== | ||
+ | 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. | ||
==About this Structure== | ==About this Structure== | ||
- | 3BOB is a [ | + | 3BOB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thalassiosira_weissflogii Thalassiosira weissflogii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOB OCA]. |
+ | |||
+ | ==Reference== | ||
+ | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18322527 18322527] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thalassiosira weissflogii]] | [[Category: Thalassiosira weissflogii]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:00:17 2008'' |
Revision as of 17:00, 20 March 2008
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, resolution 1.45Å | |||||||
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Sites: | |||||||
Ligands: | |||||||
Gene: | cdca1 (Thalassiosira weissflogii) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 2
Overview
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.
About this Structure
3BOB is a Single protein structure of sequence from Thalassiosira weissflogii. Full crystallographic information is available from OCA.
Reference
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
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