3boe: Difference between revisions

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[[Image:3boe.jpg|left|200px]]<br /><applet load="3boe" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:3boe.jpg|left|200px]]
caption="3boe, resolution 1.40&Aring;" />
 
'''Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 2 with acetate (CDCA1-R2)'''<br />
{{Structure
|PDB= 3boe |SIZE=350|CAPTION= <scene name='initialview01'>3boe</scene>, resolution 1.40&Aring;
|SITE= <scene name='pdbsite=AC1:Cd+Binding+Site+For+Residue+A+1001'>AC1</scene> and <scene name='pdbsite=AC2:Act+Binding+Site+For+Residue+A+1002'>AC2</scene>
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</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 with acetate (CDCA1-R2)'''
 
 
==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==
3BOE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thalassiosira_weissflogii Thalassiosira weissflogii] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Cd+Binding+Site+For+Residue+A+1001'>AC1</scene> and <scene name='pdbsite=AC2:Act+Binding+Site+For+Residue+A+1002'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOE OCA].  
3BOE 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=3BOE 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]]


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Revision as of 20:00, 20 March 2008

File:3boe.jpg


PDB ID 3boe

Drag the structure with the mouse to rotate
, resolution 1.40Å
Sites: and
Ligands: and
Gene: cdca1 (Thalassiosira weissflogii)
Coordinates: save as pdb, mmCIF, xml



Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 2 with acetate (CDCA1-R2)


OverviewOverview

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 StructureAbout this Structure

3BOE 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

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