5yvs

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==Crystal Structure of the archaeal halo-thermophilic Red Sea brine pool alcohol dehydrogenase ADH/D1 bound to NADP==
==Crystal Structure of the archaeal halo-thermophilic Red Sea brine pool alcohol dehydrogenase ADH/D1 bound to NADP==
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<StructureSection load='5yvs' size='340' side='right' caption='[[5yvs]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
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<StructureSection load='5yvs' size='340' side='right'caption='[[5yvs]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yvs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candidate_divison_msbl1_archaeon_scgc-aaa259e19 Candidate divison msbl1 archaeon scgc-aaa259e19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YVS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yvs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidate_division_MSBL1_archaeon_SCGC-AAA259E19 Candidate division MSBL1 archaeon SCGC-AAA259E19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YVS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.345&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5yvm|5yvm]], [[5yvr|5yvr]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AKJ65_00115 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1698264 candidate divison MSBL1 archaeon SCGC-AAA259E19])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yvs OCA], [https://pdbe.org/5yvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yvs RCSB], [https://www.ebi.ac.uk/pdbsum/5yvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yvs ProSAT]</span></td></tr>
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<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=5yvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yvs OCA], [http://pdbe.org/5yvs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yvs RCSB], [http://www.ebi.ac.uk/pdbsum/5yvs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yvs ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A133UP32_9EURY A0A133UP32_9EURY]
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Because only 0.01% of prokaryotic genospecies can be cultured and in situ observations are often impracticable, culture-independent methods are required to understand microbial life and harness potential applications of microbes. Here, we report a methodology for the production of proteins with desired functions based on single amplified genomes (SAGs) from unculturable species. We use this method to resurrect an alcohol dehydrogenase (ADH/D1) from an uncharacterized halo-thermophilic archaeon collected from a brine pool at the bottom of the Red Sea. Our crystal structure of 5,6-dihydroxy NADPH-bound ADH/D1 combined with biochemical analyses reveal the molecular features of its halo-thermophily, its unique habitat adaptations, and its possible reaction mechanism for atypical oxygen activation. Our strategy offers a general guide for using SAGs as a source for scientific and industrial investigations of "microbial dark matter."
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Identification and Experimental Characterization of an Extremophilic Brine Pool Alcohol Dehydrogenase from Single Amplified Genomes.,Grotzinger SW, Karan R, Strillinger E, Bader S, Frank A, Al Rowaihi IS, Akal A, Wackerow W, Archer JA, Rueping M, Weuster-Botz D, Groll M, Eppinger J, Arold ST ACS Chem Biol. 2017 Dec 18. doi: 10.1021/acschembio.7b00792. PMID:29188989<ref>PMID:29188989</ref>
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==See Also==
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5yvs" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Candidate divison msbl1 archaeon scgc-aaa259e19]]
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[[Category: Candidate division MSBL1 archaeon SCGC-AAA259E19]]
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[[Category: Arold, S T]]
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[[Category: Large Structures]]
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[[Category: Eppinger, J]]
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[[Category: Arold ST]]
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[[Category: Frank, A]]
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[[Category: Eppinger J]]
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[[Category: Groetzinger, S W]]
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[[Category: Frank A]]
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[[Category: Groll, M]]
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[[Category: Groetzinger SW]]
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[[Category: Strillinger, E]]
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[[Category: Groll M]]
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[[Category: Dehydrogenase]]
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[[Category: Strillinger E]]
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[[Category: Halophilic]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Protein-cofactor complex]]
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[[Category: Thermophilic]]
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Current revision

Crystal Structure of the archaeal halo-thermophilic Red Sea brine pool alcohol dehydrogenase ADH/D1 bound to NADP

PDB ID 5yvs

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