1GGW

CDC4P FROM SCHIZOSACCHAROMYCES POMBE

1GGW の概要

• エントリーDOI: 10.2210/pdb1ggw/pdb
• 分子名称: PROTEIN (CDC4P) (1 entity in total)
• 機能のキーワード: light chain, cytokinesis, cell cycle, ef-hand, cytokine
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• 細胞内の位置: Cytoplasm: Q09196
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15543.48

構造登録者

Slupsky, C.M.,Hemmingsen, S.M.,McIntosh, L.P. (登録日: 2000-09-25, 公開日: 2001-03-21, 最終更新日: 2023-12-27)

主引用文献

Slupsky, C.M.,Desautels, M.,Huebert, T.,Zhao, R.,Hemmingsen, S.M.,McIntosh, L.P.
Structure of Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe.
J.Biol.Chem., 276:5943-5951, 2001

PubMed Abstract: The Schizosaccharomyces pombe Cdc4 protein is required for the formation and function of the contractile ring, presumably acting as a myosin light chain. By using NMR spectroscopy, we demonstrate that purified Cdc4p is a monomeric protein with two structurally independent domains, each exhibiting a fold reminiscent of the EF-hand class of calcium-binding proteins. Although Cdc4p has one potentially functional calcium-binding site, it does not bind calcium in vitro. Three variants of Cdc4p containing single point mutations responsible for temperature-sensitive arrest of the cell cycle at cytokinesis (Gly-19 to Glu, Gly-82 to Asp, and Gly-107 to Ser) were also characterized by NMR and circular dichroism spectroscopy. In each case, the amino acid substitution only leads to small perturbations in the conformation of the protein. Furthermore, thermal unfolding studies indicate that, like wild-type Cdc4p, the three mutant forms are all extremely stable, remaining completely folded at temperatures significantly above those causing failure of cytokinesis in intact cells. Therefore, the altered phenotype must arise directly from a disruption of the function of Cdc4p rather than indirectly through a disruption of its overall structure. Several mutant alleles of Cdc4p also show interallelic complementation in diploid cells. This phenomenon can be explained if Cdcp4 has more than one essential function or, alternatively, if two mutant proteins assemble to form a functional complex. Based on the structure of Cdc4p, possible models for interallelic complementation including interactions with partner proteins and the formation of a myosin complex with Cdc4p fulfilling the role of both an essential and regulatory light chain are proposed.

PubMed: 11087750
DOI: 10.1074/jbc.M008716200

実験手法

SOLUTION NMR