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| | <StructureSection load='5x6j' size='340' side='right'caption='[[5x6j]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5x6j' size='340' side='right'caption='[[5x6j]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x6j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_23301 Atcc 23301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X6J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x6j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sporosarcina_globispora Sporosarcina globispora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X6J FirstGlance]. <br> |
| - | </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=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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x6i|5x6i]], [[5x6k|5x6k]], [[5x6l|5x6l]]</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=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1459 ATCC 23301])</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=5x6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6j OCA], [https://pdbe.org/5x6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x6j RCSB], [https://www.ebi.ac.uk/pdbsum/5x6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6j ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </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=5x6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6j OCA], [http://pdbe.org/5x6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x6j RCSB], [http://www.ebi.ac.uk/pdbsum/5x6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KAD_SPOGL KAD_SPOGL]] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | + | [https://www.uniprot.org/uniprot/KAD_SPOGL KAD_SPOGL] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. |
| | <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: Adenylate kinase]] | |
| - | [[Category: Atcc 23301]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bae, E]] | + | [[Category: Sporosarcina globispora]] |
| - | [[Category: Moon, S]] | + | [[Category: Bae E]] |
| - | [[Category: Atp binding]] | + | [[Category: Moon S]] |
| - | [[Category: Phosphotransferase activity]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
KAD_SPOGL Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Publication Abstract from PubMed
Protein thermal stability is an important field since thermally stable proteins are desirable in many academic and industrial settings. Information on protein thermal stabilization can be obtained by comparing homologous proteins from organisms living at distinct temperatures. Here, we report structural and mutational analyses of adenylate kinases (AKs) from psychrophilic Bacillus globisporus (AKp) and mesophilic Bacillus subtilis (AKm). Sequence and structural comparison showed suboptimal hydrophobic packing around Thr26 in the CORE domain of AKp, which was replaced with an Ile residue in AKm. Mutations that improved hydrophobicity of the Thr residue increased the thermal stability of the psychrophilic AKp, and the largest stabilization was observed for a Thr-to-Ile substitution. Furthermore, a reverse Ile-to-Thr mutation in the mesophilic AKm significantly decreased thermal stability. We determined the crystal structures of mutant AKs to confirm the impact of the residue substitutions on the overall stability. Taken together, our results provide a structural basis for the stability difference between psychrophilic and mesophilic AK homologues and highlight the role of hydrophobic interactions in protein thermal stability.
Structural and mutational analyses of psychrophilic and mesophilic adenylate kinases highlight the role of hydrophobic interactions in protein thermal stability.,Moon S, Kim J, Koo J, Bae E Struct Dyn. 2019 Mar 25;6(2):024702. doi: 10.1063/1.5089707. eCollection 2019, Mar. PMID:31111079[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moon S, Kim J, Koo J, Bae E. Structural and mutational analyses of psychrophilic and mesophilic adenylate kinases highlight the role of hydrophobic interactions in protein thermal stability. Struct Dyn. 2019 Mar 25;6(2):024702. doi: 10.1063/1.5089707. eCollection 2019, Mar. PMID:31111079 doi:http://dx.doi.org/10.1063/1.5089707
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