3boj: Difference between revisions
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<StructureSection load='3boj' size='340' side='right' caption='[[3boj]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='3boj' size='340' side='right' caption='[[3boj]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3boj]] is a 1 chain structure | <table><tr><td colspan='2'>[[3boj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BOJ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bob|3bob]], [[3boc|3boc]], [[3boe|3boe]], [[3boh|3boh]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bob|3bob]], [[3boc|3boc]], [[3boe|3boe]], [[3boh|3boh]]</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='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=3boj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boj OCA], [http://pdbe.org/3boj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3boj RCSB], [http://www.ebi.ac.uk/pdbsum/3boj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3boj ProSAT]</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=3boj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boj OCA], [http://pdbe.org/3boj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3boj RCSB], [http://www.ebi.ac.uk/pdbsum/3boj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3boj ProSAT]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Feng, L]] | [[Category: Feng, L]] | ||
[[Category: Jeffrey, P D]] | [[Category: Jeffrey, P D]] | ||
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[[Category: Carbonic anhydrase]] | [[Category: Carbonic anhydrase]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Marine diatom]] | |||
Revision as of 10:33, 31 October 2018
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)
Structural highlights
Publication Abstract from PubMedCarbonic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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