3tn7: Difference between revisions
New page: '''Unreleased structure''' The entry 3tn7 is ON HOLD Authors: Boyko, K.M., Polyakov, K.M., Bezsudnova, E.Y., Stekhanova, T.N., Gumerov, V.M., Mardanov, A.V., Ravin, N.V., Skryabin, K.G.... |
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The | ==Crystal structure of short-chain alcohol dehydrogenase from hyperthermophilic archaeon Thermococcus sibiricus complexed with 5-hydroxy-NADP== | ||
<StructureSection load='3tn7' size='340' side='right'caption='[[3tn7]], [[Resolution|resolution]] 1.68Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tn7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_sibiricus_MM_739 Thermococcus sibiricus MM 739]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TN7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NJP:5-HYDROXY-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NJP</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=3tn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tn7 OCA], [https://pdbe.org/3tn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tn7 RCSB], [https://www.ebi.ac.uk/pdbsum/3tn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tn7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C6A190_THESM C6A190_THESM] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Biochemical analysis of enantioselective short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus (TsAdh319) revealed unique polyextremophilic properties of the enzyme - half-life of 1 h at 100 degrees C, tolerance to high salt (up to 4 M) and organic solvents (50% v/v) concentrations. To elucidate the molecular basis of TsAdh319 polyextremophilicity, we determined the crystal structure of the enzyme in a binary complex with 5-hydroxy-NADP at 1.68 A resolution. TsAdh319 has a tetrameric structure both in the crystals and in solution with an intersubunit disulfide bond. The substrate-binding pocket is hydrophobic, spacious and open that is consistent with the observed promiscuity in substrate specificity of TsAdh319. The present study revealed an extraordinary number of charged residues on the surface of TsAdh319, 70% of which were involved in ion pair interactions. Further we compared the structure of TsAdh319 with the structures of other homologous short-chain dehydrogenases/reductases (SDRs) from thermophilic and mesophilic organisms. We found that TsAdh319 has the highest arginine and aspartate + glutamate contents compared to the counterparts. The frequency of occurrence of salt bridges on the surface of TsAdh319 is the highest among the SDRs under consideration. No differences in the proline, tryptophan, and phenylalanine contents are observed; the compactness of the protein core of TsAdh319, the monomer and tetramer organization do not differ from that of the counterparts. We suggest that the unique thermostability of TsAdh319 is associated with the rigidity and simultaneous "resilience" of the structure provided by a compact hydrophobic core and a large number of surface ion pairs. An extensive salt bridge network also might maintain the structural integrity of TsAdh319 in high salinity. | |||
Structural insight into the molecular basis of polyextremophilicity of short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus.,Bezsudnova EY, Boyko KM, Polyakov KM, Dorovatovskiy PV, Stekhanova TN, Gumerov VM, Ravin NV, Skryabin KG, Kovalchuk MV, Popov VO Biochimie. 2012 Dec;94(12):2628-38. doi: 10.1016/j.biochi.2012.07.024. Epub 2012 , Aug 5. PMID:22885278<ref>PMID:22885278</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3tn7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermococcus sibiricus MM 739]] | |||
[[Category: Bezsudnova EY]] | |||
[[Category: Boyko KM]] | |||
[[Category: Gumerov VM]] | |||
[[Category: Kovalchuk MV]] | |||
[[Category: Mardanov AV]] | |||
[[Category: Polyakov KM]] | |||
[[Category: Popov VO]] | |||
[[Category: Ravin NV]] | |||
[[Category: Skryabin KG]] | |||
[[Category: Stekhanova TN]] | |||
Latest revision as of 09:12, 17 October 2024
Crystal structure of short-chain alcohol dehydrogenase from hyperthermophilic archaeon Thermococcus sibiricus complexed with 5-hydroxy-NADPCrystal structure of short-chain alcohol dehydrogenase from hyperthermophilic archaeon Thermococcus sibiricus complexed with 5-hydroxy-NADP
Structural highlights
FunctionPublication Abstract from PubMedBiochemical analysis of enantioselective short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus (TsAdh319) revealed unique polyextremophilic properties of the enzyme - half-life of 1 h at 100 degrees C, tolerance to high salt (up to 4 M) and organic solvents (50% v/v) concentrations. To elucidate the molecular basis of TsAdh319 polyextremophilicity, we determined the crystal structure of the enzyme in a binary complex with 5-hydroxy-NADP at 1.68 A resolution. TsAdh319 has a tetrameric structure both in the crystals and in solution with an intersubunit disulfide bond. The substrate-binding pocket is hydrophobic, spacious and open that is consistent with the observed promiscuity in substrate specificity of TsAdh319. The present study revealed an extraordinary number of charged residues on the surface of TsAdh319, 70% of which were involved in ion pair interactions. Further we compared the structure of TsAdh319 with the structures of other homologous short-chain dehydrogenases/reductases (SDRs) from thermophilic and mesophilic organisms. We found that TsAdh319 has the highest arginine and aspartate + glutamate contents compared to the counterparts. The frequency of occurrence of salt bridges on the surface of TsAdh319 is the highest among the SDRs under consideration. No differences in the proline, tryptophan, and phenylalanine contents are observed; the compactness of the protein core of TsAdh319, the monomer and tetramer organization do not differ from that of the counterparts. We suggest that the unique thermostability of TsAdh319 is associated with the rigidity and simultaneous "resilience" of the structure provided by a compact hydrophobic core and a large number of surface ion pairs. An extensive salt bridge network also might maintain the structural integrity of TsAdh319 in high salinity. Structural insight into the molecular basis of polyextremophilicity of short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus.,Bezsudnova EY, Boyko KM, Polyakov KM, Dorovatovskiy PV, Stekhanova TN, Gumerov VM, Ravin NV, Skryabin KG, Kovalchuk MV, Popov VO Biochimie. 2012 Dec;94(12):2628-38. doi: 10.1016/j.biochi.2012.07.024. Epub 2012 , Aug 5. PMID:22885278[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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