1IT6

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

1IT6 の概要

• エントリーDOI: 10.2210/pdb1it6/pdb
• 分子名称: SERINE/THREONINE PROTEIN PHOSPHATASE 1 GAMMA (PP1-GAMMA) CATALYTIC SUBUNIT, MANGANESE (II) ION, CALYCULIN A, ... (4 entities in total)
• 機能のキーワード: hydrolase-inhibitor complex, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P36873
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76299.65

構造登録者

Kita, A.,Matsunaga, S.,Takai, A.,Kataiwa, H.,Wakimoto, T.,Fusetani, N.,Isobe, M.,Miki, K. (登録日: 2002-01-09, 公開日: 2002-05-22, 最終更新日: 2023-10-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)