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| | <StructureSection load='6sc4' size='340' side='right'caption='[[6sc4]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6sc4' size='340' side='right'caption='[[6sc4]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sc4]] is a 5 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=6SC4 FirstGlance]. <br> | + | <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='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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v3w|1v3w]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AKJ37_07020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1698267 candidate division MSBL1 archaeon SCGC-AAA259I09])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sc4 OCA], [http://pdbe.org/6sc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sc4 RCSB], [http://www.ebi.ac.uk/pdbsum/6sc4 PDBsum], [http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Candidate division msbl1 archaeon scgc-aaa259i09]] | + | [[Category: Candidate division MSBL1 archaeon SCGC-AAA259I09]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: DasSarma, P]] | + | [[Category: Das Sarma S]] |
| - | [[Category: Eppinger, J]] | + | [[Category: DasSarma P]] |
| - | [[Category: Groetzinger, S W]] | + | [[Category: Eppinger J]] |
| - | [[Category: Groll, M]] | + | [[Category: Groetzinger SW]] |
| - | [[Category: Karan, R]] | + | [[Category: Groll M]] |
| - | [[Category: Renn, D]] | + | [[Category: Karan R]] |
| - | [[Category: Rueping, M]] | + | [[Category: Renn D]] |
| - | [[Category: Sarma, S Das]]
| + | [[Category: Rueping M]] |
| - | [[Category: Vancea, A]] | + | [[Category: Vancea A]] |
| - | [[Category: Vielberg, V T]] | + | [[Category: Vielberg V-T]] |
| - | [[Category: Vogler, M]] | + | [[Category: Vogler M]] |
| - | [[Category: Enzyme engineering]]
| + | |
| - | [[Category: Halophile]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Red sea brine pool discovery deep]]
| + | |
| - | [[Category: Salt adaptation]]
| + | |
| Structural highlights
6sc4 is a 5 chain structure with sequence from Candidate division MSBL1 archaeon SCGC-AAA259I09. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.6Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A133ULQ3_9EURY
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vogler M, Karan R, Renn D, Vancea A, Vielberg MT, Grotzinger SW, DasSarma P, DasSarma S, Eppinger J, Groll M, Rueping M. Crystal Structure and Active Site Engineering of a Halophilic gamma-Carbonic Anhydrase. Front Microbiol. 2020 Apr 28;11:742. doi: 10.3389/fmicb.2020.00742. eCollection, 2020. PMID:32411108 doi:http://dx.doi.org/10.3389/fmicb.2020.00742
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