9w00: Difference between revisions
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==Crystal structure of C-terminal domain of theta type Carbonic Anhydrase 3 from marine diatom Phaeodactylum tricornutum== | |||
<StructureSection load='9w00' size='340' side='right'caption='[[9w00]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9w00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phaeodactylum_tricornutum Phaeodactylum tricornutum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9W00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9W00 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9w00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9w00 OCA], [https://pdbe.org/9w00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9w00 RCSB], [https://www.ebi.ac.uk/pdbsum/9w00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9w00 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A173M023_PHATR A0A173M023_PHATR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Carbonic anhydrase (CA) catalyzes the reversible hydration of carbon dioxide (CO(2)) to bicarbonate (HCO(3) (-)) and plays an essential role in carbon fixation in marine diatoms. Here we report the structural and functional characterization of a novel CA, theta-CA3, from the diatom Phaeodactylum tricornutum, elucidating its physiological role and catalytic mechanism. AlphaFold prediction, sequence alignment, and metal analysis showed that theta-CA3 is a dimeric enzyme, with each monomer composed of two zinc-binding catalytic domains. High-resolution X-ray crystallographic structures of domain 2 of theta-CA3 in the CO(2)-bound form revealed the detailed substrate binding pattern in the active site. Site-directed mutagenesis showed that Asp49 and Arg117 in the active site are essential for catalysis. Notably, introducing a negative charge near the active-site entrance resulted in a mutant enzyme with markedly increased activity under acidic pH, suggesting that electrostatic modulation of the active-site environment regulates proton transfer and catalysis. Furthermore, we identified an HCO(3) (-) ion at the dimer interface that contributes to enzyme activation. Collectively, our findings provide fundamental structural insight into how the active-site electrostatic charges and metal environment govern the catalytic efficiency of theta-CA3, offering a new perspective on the molecular basis of carbon fixation in diatoms. | |||
Structural insights into theta-type carbonic anhydrases 3 and 4: Tuning the directionality of CO(2) hydration in a diatom.,Negoro H, Ohsawa A, Shimakawa G, Tanaka H, Matsuda Y, Kurisu G FEBS J. 2026 Jul 14. doi: 10.1111/febs.70654. PMID:42447277<ref>PMID:42447277</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9w00" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Phaeodactylum tricornutum]] | |||
[[Category: Kurisu G]] | |||
[[Category: Negoro H]] | |||
[[Category: Tanaka H]] | |||
Latest revision as of 20:29, 29 July 2026
Crystal structure of C-terminal domain of theta type Carbonic Anhydrase 3 from marine diatom Phaeodactylum tricornutum
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