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| | <StructureSection load='4cnx' size='340' side='right'caption='[[4cnx]], [[Resolution|resolution]] 1.23Å' scene=''> | | <StructureSection load='4cnx' size='340' side='right'caption='[[4cnx]], [[Resolution|resolution]] 1.23Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cnx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CNX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CNX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cnx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CNX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <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]] 1.23Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cnr|4cnr]], [[4cnv|4cnv]], [[4cnw|4cnw]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4cnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnx OCA], [https://pdbe.org/4cnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cnx RCSB], [https://www.ebi.ac.uk/pdbsum/4cnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cnx 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=4cnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnx OCA], [http://pdbe.org/4cnx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cnx RCSB], [http://www.ebi.ac.uk/pdbsum/4cnx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cnx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAH2_BOVIN CAH2_BOVIN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. | + | [https://www.uniprot.org/uniprot/CAH2_BOVIN CAH2_BOVIN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: Carbonate dehydratase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dojchinov, G]] | + | [[Category: Dojchinov G]] |
| - | [[Category: Haritos, V]] | + | [[Category: Haritos V]] |
| - | [[Category: Newman, J]] | + | [[Category: Newman J]] |
| - | [[Category: Peat, T S]] | + | [[Category: Peat TS]] |
| - | [[Category: Seabrook, S]] | + | [[Category: Seabrook S]] |
| - | [[Category: Warden, A]] | + | [[Category: Warden A]] |
| - | [[Category: Williams, M]] | + | [[Category: Williams M]] |
| - | [[Category: Co2 capture]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Protein engineering]]
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| Structural highlights
Function
CAH2_BOVIN Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide.
Publication Abstract from PubMed
Enzymes expressed by highly salt-tolerant organisms show many modifications compared with salt-affected counterparts including biased amino acid and lower alpha-helix content, lower solvent accessibility and negative surface charge. Here, we show that halotolerance can be generated in an enzyme solely by modifying surface residues. Rational design of carbonic anhydrase II is undertaken in three stages replacing 18 residues in total, crystal structures confirm changes are confined to surface residues. Catalytic activities and thermal unfolding temperatures of the designed enzymes increase at high salt concentrations demonstrating their shift to halotolerance, whereas the opposite response is found in the wild-type enzyme. Molecular dynamics calculations reveal a key role for sodium ions in increasing halotolerant enzyme stability largely through interactions with the highly ordered first Na(+) hydration shell. For the first time, an approach to generate extreme halotolerance, a trait with broad application in industrial biocatalysis, in a wild-type enzyme is demonstrated.
Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst.,Warden AC, Williams M, Peat TS, Seabrook SA, Newman J, Dojchinov G, Haritos VS Nat Commun. 2015 Dec 21;6:10278. doi: 10.1038/ncomms10278. PMID:26687908[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Warden AC, Williams M, Peat TS, Seabrook SA, Newman J, Dojchinov G, Haritos VS. Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst. Nat Commun. 2015 Dec 21;6:10278. doi: 10.1038/ncomms10278. PMID:26687908 doi:http://dx.doi.org/10.1038/ncomms10278
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