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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ddz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyridium_purpureum Porphyridium purpureum]. The January 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Carbonic Anhydrase''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_1 10.2210/rcsb_pdb/mom_2004_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DDZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ddz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyridium_purpureum Porphyridium purpureum]. The January 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Carbonic Anhydrase''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_1 10.2210/rcsb_pdb/mom_2004_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DDZ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1ddz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ddz OCA], [https://pdbe.org/1ddz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ddz RCSB], [https://www.ebi.ac.uk/pdbsum/1ddz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ddz ProSAT]</span></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=1ddz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ddz OCA], [https://pdbe.org/1ddz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ddz RCSB], [https://www.ebi.ac.uk/pdbsum/1ddz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ddz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q43060_PORPP Q43060_PORPP]  
[https://www.uniprot.org/uniprot/Q43060_PORPP Q43060_PORPP]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The carbonic anhydrases (CAs) fall into three evolutionarily distinct families designated alpha-, beta-, and gamma-CAs based on their primary structure. beta-CAs are present in higher plants, algae, and prokaryotes, and are involved in inorganic carbon utilization. Here, we describe the novel x-ray structure of beta-CA from the red alga, Porphyridium purpureum, at 2.2-A resolution using intrinsic zinc multiwavelength anomalous diffraction phasing. The CA monomer is composed of two internally repeating structures, being folded as a pair of fundamentally equivalent motifs of an alpha/beta domain and three projecting alpha-helices. The motif is obviously distinct from that of either alpha- or gamma-CAs. This homodimeric CA appears like a tetramer with a pseudo 222 symmetry. The active site zinc is coordinated by a Cys-Asp-His-Cys tetrad that is strictly conserved among the beta-CAs. No water molecule is found in a zinc-liganding radius, indicating that the zinc-hydroxide mechanism in alpha-CAs, and possibly in gamma-CAs, is not directly applicable to the case in beta-CAs. Zinc coordination environments of the CAs provide an interesting example of the convergent evolution of distinct catalytic sites required for the same CO(2) hydration reaction.
X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration.,Mitsuhashi S, Mizushima T, Yamashita E, Yamamoto M, Kumasaka T, Moriyama H, Ueki T, Miyachi S, Tsukihara T J Biol Chem. 2000 Feb 25;275(8):5521-6. PMID:10681531<ref>PMID:10681531</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ddz" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 06:52, 7 February 2024

X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1

1ddz, resolution 2.20Å

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