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| | ==Crystal structure of adenylate kinase== | | ==Crystal structure of adenylate kinase== |
| - | <StructureSection load='5x6k' size='340' side='right' caption='[[5x6k]], [[Resolution|resolution]] 1.99Å' scene=''> | + | <StructureSection load='5x6k' size='340' side='right'caption='[[5x6k]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Notothenia_coriiceps Notothenia coriiceps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X6K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x6k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Notothenia_coriiceps Notothenia coriiceps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X6K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.99Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x6l|5x6l]], [[5x6j|5x6j]], [[5x6i|5x6i]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <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=5x6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6k OCA], [http://pdbe.org/5x6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x6k RCSB], [http://www.ebi.ac.uk/pdbsum/5x6k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6k ProSAT]</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=5x6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6k OCA], [https://pdbe.org/5x6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x6k RCSB], [https://www.ebi.ac.uk/pdbsum/5x6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A2R2JFU5_9TELE A0A2R2JFU5_9TELE] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.[HAMAP-Rule:MF_03171] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Adenylate kinase|Adenylate kinase]] | + | *[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Notothenia coriiceps]] | | [[Category: Notothenia coriiceps]] |
| - | [[Category: Bae, E]] | + | [[Category: Bae E]] |
| - | [[Category: Moon, S]] | + | [[Category: Moon S]] |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
A0A2R2JFU5_9TELE Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.[HAMAP-Rule:MF_03171]
Publication Abstract from PubMed
Psychrophiles are extremophilic organisms capable of thriving in cold environments. Proteins from these cold-adapted organisms can remain physiologically functional at low temperatures, but are structurally unstable even at moderate temperatures. Here, we report the crystal structure of adenylate kinase (AK) from the Antarctic fish Notothenia coriiceps, and identify the structural basis of cold adaptation by comparison with homologues from tropical fishes including Danio rerio. The structure of N. coriiceps AK (AKNc) revealed suboptimal hydrophobic packing around three Val residues in its central CORE domain, which are replaced with Ile residues in D. rerio AK (AKDr). The Val-to-Ile mutations that improve hydrophobic CORE packing in AKNc increased stability at high temperatures but decreased activity at low temperatures, suggesting that the suboptimal hydrophobic CORE packing is important for cold adaptation. Such linkage between stability and activity was also observed in AKDr. Ile-to-Val mutations that destabilized the tropical AK resulted in increased activity at low temperatures. Our results provide the structural basis of cold adaptation of a psychrophilic enzyme from a multicellular, eukaryotic organism, and highlight the similarities and differences in the structural adjustment of vertebrate and bacterial psychrophilic AKs during cold adaptation.
Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes.,Moon S, Kim J, Bae E Sci Rep. 2017 Nov 22;7(1):16027. doi: 10.1038/s41598-017-16266-9. PMID:29167503[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moon S, Kim J, Bae E. Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes. Sci Rep. 2017 Nov 22;7(1):16027. doi: 10.1038/s41598-017-16266-9. PMID:29167503 doi:http://dx.doi.org/10.1038/s41598-017-16266-9
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