4x5s: Difference between revisions

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New page: '''Unreleased structure''' The entry 4x5s is ON HOLD Authors: De Simone, G., Alterio, V., Di Fiore, A. Description: The crystal structure of an alpha carbonic anhydrase from the extrem...
 
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'''Unreleased structure'''


The entry 4x5s is ON HOLD
==The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.==
<StructureSection load='4x5s' size='340' side='right'caption='[[4x5s]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4x5s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurihydrogenibium_azorense Sulfurihydrogenibium azorense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X5S 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</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=4x5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5s OCA], [https://pdbe.org/4x5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x5s RCSB], [https://www.ebi.ac.uk/pdbsum/4x5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5s ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C1DTU5_SULAA C1DTU5_SULAA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two thermostable alpha-carbonic anhydrases (alpha-CAs) isolated from thermophilic Sulfurihydrogenibium spp., namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active alpha-CA known to date for the CO2 hydration reaction. Here we report the crystallographic structure of SazCA and the identification of the structural features responsible for its high catalytic activity, by comparing it with SspCA structure. These data are of relevance for the design of engineered proteins showing higher stability and catalytic activity than other alpha-CAs known to date.


Authors: De Simone, G., Alterio, V., Di Fiore, A.
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense.,De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A Bioorg Med Chem Lett. 2015 May 1;25(9):2002-6. doi: 10.1016/j.bmcl.2015.02.068., Epub 2015 Mar 6. PMID:25817590<ref>PMID:25817590</ref>


Description: The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4x5s" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfurihydrogenibium azorense]]
[[Category: Alterio V]]
[[Category: De Simone G]]
[[Category: Di Fiore A]]

Latest revision as of 13:47, 10 January 2024

The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.

Structural highlights

4x5s is a 2 chain structure with sequence from Sulfurihydrogenibium azorense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C1DTU5_SULAA

Publication Abstract from PubMed

Two thermostable alpha-carbonic anhydrases (alpha-CAs) isolated from thermophilic Sulfurihydrogenibium spp., namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active alpha-CA known to date for the CO2 hydration reaction. Here we report the crystallographic structure of SazCA and the identification of the structural features responsible for its high catalytic activity, by comparing it with SspCA structure. These data are of relevance for the design of engineered proteins showing higher stability and catalytic activity than other alpha-CAs known to date.

Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense.,De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A Bioorg Med Chem Lett. 2015 May 1;25(9):2002-6. doi: 10.1016/j.bmcl.2015.02.068., Epub 2015 Mar 6. PMID:25817590[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A. Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense. Bioorg Med Chem Lett. 2015 May 1;25(9):2002-6. doi: 10.1016/j.bmcl.2015.02.068., Epub 2015 Mar 6. PMID:25817590 doi:http://dx.doi.org/10.1016/j.bmcl.2015.02.068

4x5s, resolution 1.95Å

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