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| | <StructureSection load='1y7w' size='340' side='right'caption='[[1y7w]], [[Resolution|resolution]] 1.86Å' scene=''> | | <StructureSection load='1y7w' size='340' side='right'caption='[[1y7w]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y7w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dunsa Dunsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y7W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y7w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dunaliella_salina Dunaliella salina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y7W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.86Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dCA II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3046 DUNSA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1y7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y7w OCA], [https://pdbe.org/1y7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y7w RCSB], [https://www.ebi.ac.uk/pdbsum/1y7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y7w ProSAT], [https://www.topsan.org/Proteins/ISPC/1y7w TOPSAN]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y7w OCA], [http://pdbe.org/1y7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y7w RCSB], [http://www.ebi.ac.uk/pdbsum/1y7w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y7w ProSAT], [http://www.topsan.org/Proteins/ISPC/1y7w TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carbonate dehydratase]] | + | [[Category: Dunaliella salina]] |
| - | [[Category: Dunsa]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bageshwar, U K]] | + | [[Category: Bageshwar UK]] |
| - | [[Category: Gokhman, I]] | + | [[Category: Gokhman I]] |
| - | [[Category: Greenblatt, H M]] | + | [[Category: Greenblatt HM]] |
| - | [[Category: ISPC, Israel Structural Proteomics Center]]
| + | [[Category: Premkumar L]] |
| - | [[Category: Premkumar, L]] | + | [[Category: Savchenko T]] |
| - | [[Category: Savchenko, T]] | + | [[Category: Sussman JL]] |
| - | [[Category: Sussman, J L]] | + | [[Category: Zamir A]] |
| - | [[Category: Zamir, A]] | + | |
| - | [[Category: Algal carbonic anhydrase]]
| + | |
| - | [[Category: Alpha-type carbonic anhydrase]]
| + | |
| - | [[Category: Anion tolerance]]
| + | |
| - | [[Category: Dca ii]]
| + | |
| - | [[Category: Dunaliella salina carbonic anhydrase]]
| + | |
| - | [[Category: Haltolerant protein]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Salt tolerant protein]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Zinc enzyme]]
| + | |
| Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein molecular adaptation to drastically shifting salinities was studied in dCA II, an alpha-type carbonic anhydrase (EC 4.2.1.1) from the exceptionally salt-tolerant unicellular green alga Dunaliella salina. The salt-inducible, extracellular dCA II is highly salt-tolerant and thus differs from its mesophilic homologs. The crystal structure of dCA II, determined at 1.86-A resolution, is globally similar to other alpha-type carbonic anhydrases except for two extended alpha-helices and an added Na-binding loop. Its unusual electrostatic properties include a uniformly negative surface electrostatic potential of lower magnitude than that observed in the highly acidic halophilic proteins and an exceptionally low positive potential at a site adjoining the catalytic Zn(2+) compared with mesophilic homologs. The halotolerant dCA II also differs from typical halophilic proteins in retaining conformational stability and solubility in low to high salt concentrations. The crucial role of electrostatic features in dCA II halotolerance is strongly supported by the ability to predict the unanticipated halotolerance of the murine CA XIV isozyme, which was confirmed biochemically. A proposal for the functional significance of the halotolerance of CA XIV in the kidney is presented.
Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog.,Premkumar L, Greenblatt HM, Bageshwar UK, Savchenko T, Gokhman I, Sussman JL, Zamir A Proc Natl Acad Sci U S A. 2005 May 24;102(21):7493-8. Epub 2005 May 13. PMID:15894606[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Premkumar L, Greenblatt HM, Bageshwar UK, Savchenko T, Gokhman I, Sussman JL, Zamir A. Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog. Proc Natl Acad Sci U S A. 2005 May 24;102(21):7493-8. Epub 2005 May 13. PMID:15894606 doi:0502829102
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