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2737: Revisiting Puzzle 77: Copper Chaperone

Closed since about 2 months ago

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Summary

Created
March 11, 2026
Expires
Max points
100
Description

This is a throwback puzzle to the early days of Foldit. This protein binds copper ions so that they may be transported safely to the cell compartments and enzymes that require them. The protein is modeled here in the reduced state, so no disulfides are expected to form. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

Sequence
AQEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI

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Comments

Serca Lv 1

This protein functions as a vital intracellular copper chaperone, acting as a molecular escort that safely transports toxic, highly reactive copper ions through the cell. Structurally, this small protein folds into an "open beta-sandwich" architecture, but its true functional power lies in a highly conserved Cys-X-X-Cys motif located on a flexible loop. Within this motif, two cysteine residues act like chemical "handcuffs," using their sulfur atoms to tightly but reversibly bind a single copper ion, neutralizing its cellular threat before delivering the payload precisely to its target enzyme.