View source for 3boc


==Carbonic anhydrase from marine diatom Thalassiosira weissflogii- zinc bound domain 2 (CDCA1-R2)==
<StructureSection load='3boc' size='340' side='right' caption='[[3boc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3boc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BOC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bob|3bob]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3boc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boc OCA], [http://pdbe.org/3boc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3boc RCSB], [http://www.ebi.ac.uk/pdbsum/3boc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3boc ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:18322527</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3boc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carbonic anhydrase|Carbonic anhydrase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Carbonate dehydratase]]
[[Category: Feng, L]]
[[Category: Jeffrey, P D]]
[[Category: Morel, F M.M]]
[[Category: Shi, Y]]
[[Category: Xu, Y]]
[[Category: Carbonic anhydrase]]
[[Category: Lyase]]
[[Category: Marine diatom]]
[[Category: Zinc-bound]]