1atp
From Proteopedia
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2.2 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A PEPTIDE INHIBITOR
Overview
. 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 A 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 Mg(2+), were soaked in Mn(2+)., Two Mn(2+) ions were identified using an anomalous Fourier map. One Mn(2+), ion bridges the gamma- and beta-phosphates and interacts with Asp184 and, two water molecules. The second Mn(2+) 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.
About this Structure
1ATP is a Protein complex structure of sequences from Mus musculus with MN, PO3 and ATP as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor., Zheng J, Trafny EA, Knighton DR, Xuong NH, Taylor SS, Ten Eyck LF, Sowadski JM, Acta Crystallogr D Biol Crystallogr. 1993 May 1;49(Pt 3):362-5. PMID:15299527
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