6sc4
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==Gamma-Carbonic Anhydrase from the Haloarchaeon Halobacterium sp.== | ==Gamma-Carbonic Anhydrase from the Haloarchaeon Halobacterium sp.== | ||
| - | <StructureSection load='6sc4' size='340' side='right'caption='[[6sc4]]' scene=''> | + | <StructureSection load='6sc4' size='340' side='right'caption='[[6sc4]], [[Resolution|resolution]] 2.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SC4 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6sc4]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidate_division_MSBL1_archaeon_SCGC-AAA259I09 Candidate division MSBL1 archaeon SCGC-AAA259I09]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SC4 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=6sc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sc4 OCA], [https://pdbe.org/6sc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sc4 RCSB], [https://www.ebi.ac.uk/pdbsum/6sc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sc4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A133ULQ3_9EURY A0A133ULQ3_9EURY] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Environments previously thought to be uninhabitable offer a tremendous wealth of unexplored microorganisms and enzymes. In this paper, we present the discovery and characterization of a novel gamma-carbonic anhydrase (gamma-CA) from the polyextreme Red Sea brine pool Discovery Deep (2141 m depth, 44.8 degrees C, 26.2% salt) by single-cell genome sequencing. The extensive analysis of the selected gene helps demonstrate the potential of this culture-independent method. The enzyme was expressed in the bioengineered haloarchaeon Halobacterium sp. NRC-1 and characterized by X-ray crystallography and mutagenesis. The 2.6 A crystal structure of the protein shows a trimeric arrangement. Within the gamma-CA, several possible structural determinants responsible for the enzyme's salt stability could be highlighted. Moreover, the amino acid composition on the protein surface and the intra- and intermolecular interactions within the protein differ significantly from those of its close homologs. To gain further insights into the catalytic residues of the gamma-CA enzyme, we created a library of variants around the active site residues and successfully improved the enzyme activity by 17-fold. As several gamma-CAs have been reported without measurable activity, this provides further clues as to critical residues. Our study reveals insights into the halophilic gamma-CA activity and its unique adaptations. The study of the polyextremophilic carbonic anhydrase provides a basis for outlining insights into strategies for salt adaptation, yielding enzymes with industrially valuable properties, and the underlying mechanisms of protein evolution. | ||
| + | |||
| + | Crystal Structure and Active Site Engineering of a Halophilic gamma-Carbonic Anhydrase.,Vogler M, Karan R, Renn D, Vancea A, Vielberg MT, Grotzinger SW, DasSarma P, DasSarma S, Eppinger J, Groll M, Rueping M Front Microbiol. 2020 Apr 28;11:742. doi: 10.3389/fmicb.2020.00742. eCollection, 2020. PMID:32411108<ref>PMID:32411108</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6sc4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Candidate division MSBL1 archaeon SCGC-AAA259I09]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Das Sarma S]] | [[Category: Das Sarma S]] | ||
Current revision
Gamma-Carbonic Anhydrase from the Haloarchaeon Halobacterium sp.
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