2CPK

CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE

Replaces:  1CPK

Summary for 2CPK

• Entry DOI: 10.2210/pdb2cpk/pdb
• Descriptor: cAMP-DEPENDENT PROTEIN KINASE, CATALYTIC SUBUNIT, PEPTIDE INHIBITOR 20-MER (2 entities in total)
• Functional Keywords: transferase(phosphotransferase)
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm (By similarity): P05132
• Total number of polymer chains: 2
• Total formula weight: 42963.71

Authors

Knighton, D.R.,Zheng, J.,Teneyck, L.F.,Ashford, V.A.,Xuong, N.-H.,Taylor, S.S.,Sowadski, J.M. (deposition date: 1992-10-21, release date: 1993-01-15, Last modification date: 2024-10-23)

Primary citation

Knighton, D.R.,Zheng, J.H.,Ten Eyck, L.F.,Ashford, V.A.,Xuong, N.H.,Taylor, S.S.,Sowadski, J.M.
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
Science, 253:407-414, 1991

PubMed Abstract: The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.

PubMed: 1862342

Experimental method

X-RAY DIFFRACTION (2.7 Å)