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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Gerlits, Oksana Das, Amit Tian, Jianhui Kovalevsky, Andrey Langan, Paul Heller, William T. |
| Description | Author Affiliation: Gerlits O ( From the Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831.); Tian J ( From the Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831.); Das A ( From the Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831.); Langan P ( From the Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831.); Heller WT ( From the Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831 hellerwt@ornl.gov.); Kovalevsky A ( From the Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831 kovalevskyay@ornl.gov.) |
| Abstract | To study the catalytic mechanism of phosphorylation catalyzed by cAMP-dependent protein kinase (PKA) a structure of the enzyme-substrate complex representing the Michaelis complex is of specific interest as it can shed light on the structure of the transition state. However, all previous crystal structures of the Michaelis complex mimics of the PKA catalytic subunit (PKAc) were obtained with either peptide inhibitors or ATP analogs. Here we utilized Ca(2+) ions and sulfur in place of the nucleophilic oxygen in a 20-residue pseudo-substrate peptide (CP20) and ATP to produce a close mimic of the Michaelis complex. In the ternary reactant complex, the thiol group of Cys-21 of the peptide is facing Asp-166 and the sulfur atom is positioned for an in-line phosphoryl transfer. Replacement of Ca(2+) cations with Mg(2+) ions resulted in a complex with trapped products of ATP hydrolysis: phosphate ion and ADP. The present structural results in combination with the previously reported structures of the transition state mimic and phosphorylated product complexes complete the snapshots of the phosphoryl transfer reaction by PKAc, providing us with the most thorough picture of the catalytic mechanism to date. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 25 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-06-19 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphate Chemistry Calcium Cyclic AMP-Dependent Protein Kinase Catalytic Subunits Magnesium Metabolism Animals Catalysis Crystallography, X-Ray Genetics Mice Phosphates Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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