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

5g41 is a 1 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.54Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Nguyen V, Wilson C, Hoemberger M, Stiller JB, Agafonov RV, Kutter S, English J, Theobald DL, Kern D. Evolutionary drivers of thermoadaptation in enzyme catalysis. Science. 2017 Jan 20;355(6322):289-294. doi: 10.1126/science.aah3717. Epub 2016, Dec 22. PMID:28008087 doi:http://dx.doi.org/10.1126/science.aah3717

5g41, resolution 1.54Å

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