1IT6

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1

Summary for 1IT6

• Entry DOI: 10.2210/pdb1it6/pdb
• Descriptor: SERINE/THREONINE PROTEIN PHOSPHATASE 1 GAMMA (PP1-GAMMA) CATALYTIC SUBUNIT, MANGANESE (II) ION, CALYCULIN A, ... (4 entities in total)
• Functional Keywords: hydrolase-inhibitor complex, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P36873
• Total number of polymer chains: 2
• Total formula weight: 76299.65

Authors

Kita, A.,Matsunaga, S.,Takai, A.,Kataiwa, H.,Wakimoto, T.,Fusetani, N.,Isobe, M.,Miki, K. (deposition date: 2002-01-09, release date: 2002-05-22, Last modification date: 2023-10-25)

Primary citation

Kita, A.,Matsunaga, S.,Takai, A.,Kataiwa, H.,Wakimoto, T.,Fusetani, N.,Isobe, M.,Miki, K.
Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1.
Structure, 10:715-724, 2002

PubMed Abstract: The crystal structure of the catalytic subunit of the protein phosphatase 1 (PP1), PP1 gamma, in complex with a marine toxin, calyculin A, was determined at 2.0 A resolution. The metal binding site contains the phosphate group of calyculin A and forms a tight network via the hydrophilic interactions between PP1 and calyculin A. Calyculin A is located in two of the three grooves, namely, in the hydrophobic groove and the acidic groove on the molecular surface. This is the first observation to note that the inhibitor adopts not a pseudocyclic conformation but an extended conformation in order to form a complex with the protein. The amino acid terminus of calyculin A contributes, in a limited manner, to the binding to PP1 gamma, which is consistent with findings from the studies of dose-inhibition analysis.

PubMed: 12015153
DOI: 10.1016/S0969-2126(02)00764-5

Experimental method

X-RAY DIFFRACTION (2 Å)