ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
. The crystal structure of a ternary complex containing the catalytic subunit of cAMP-dependent protein kinase, ATP and a 20-residue inhibitor peptide was refined at a resolution of 2.2 Å to an R value of 0.177. In order to identify the metal binding sites, the crystals, originally grown in the presence of low concentrations of Mg2+, were soaked in Mn2+. Two Mn2+ ions were identified using an anomalous Fourier map. One Mn2+ ion bridges the γ- and β-phosphates and interacts with Asp184 and two water molecules. The second Mn2+ ion interacts with the side chains of Asn171 and Asp l84 as well as with a water molecule. Modeling a serine into the P site of the inhibitor peptide suggests a mechanism for phosphotransfer.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444993000423