5g41: Difference between revisions
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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=5g41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g41 OCA], [http://pdbe.org/5g41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g41 RCSB], [http://www.ebi.ac.uk/pdbsum/5g41 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g41 ProSAT]</span></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=5g41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g41 OCA], [http://pdbe.org/5g41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g41 RCSB], [http://www.ebi.ac.uk/pdbsum/5g41 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g41 ProSAT]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
With early life likely to have existed in a hot environment, enzymes had to cope with an inherent drop in catalytic speed caused by lowered temperature. Here we characterize the molecular mechanisms underlying thermoadaptation of enzyme catalysis in adenylate kinase using ancestral sequence reconstruction spanning 3 billion years of evolution. We show that evolution solved the enzyme's key kinetic obstacle-how to maintain catalytic speed on a cooler Earth-by exploiting transition-state heat capacity. Tracing the evolution of enzyme activity and stability from the hot-start toward modern hyperthermophilic, mesophilic, and psychrophilic organisms illustrates active pressure versus passive drift in evolution on a molecular level, refutes the debated activity/stability trade-off, and suggests that the catalytic speed of adenylate kinase is an evolutionary driver for organismal fitness. | |||
Evolutionary drivers of thermoadaptation in enzyme catalysis.,Nguyen V, Wilson C, Hoemberger M, Stiller JB, Agafonov RV, Kutter S, English J, Theobald DL, Kern D Science. 2017 Jan 20;355(6322):289-294. doi: 10.1126/science.aah3717. Epub 2016, Dec 22. PMID:28008087<ref>PMID:28008087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5g41" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 10:44, 9 March 2017
Crystal structure of adenylate kinase ancestor 4 with Zn, Mg and Ap5A boundCrystal structure of adenylate kinase ancestor 4 with Zn, Mg and Ap5A bound
Structural highlights
Publication Abstract from PubMedWith early life likely to have existed in a hot environment, enzymes had to cope with an inherent drop in catalytic speed caused by lowered temperature. Here we characterize the molecular mechanisms underlying thermoadaptation of enzyme catalysis in adenylate kinase using ancestral sequence reconstruction spanning 3 billion years of evolution. We show that evolution solved the enzyme's key kinetic obstacle-how to maintain catalytic speed on a cooler Earth-by exploiting transition-state heat capacity. Tracing the evolution of enzyme activity and stability from the hot-start toward modern hyperthermophilic, mesophilic, and psychrophilic organisms illustrates active pressure versus passive drift in evolution on a molecular level, refutes the debated activity/stability trade-off, and suggests that the catalytic speed of adenylate kinase is an evolutionary driver for organismal fitness. Evolutionary drivers of thermoadaptation in enzyme catalysis.,Nguyen V, Wilson C, Hoemberger M, Stiller JB, Agafonov RV, Kutter S, English J, Theobald DL, Kern D Science. 2017 Jan 20;355(6322):289-294. doi: 10.1126/science.aah3717. Epub 2016, Dec 22. PMID:28008087[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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