8SJC

Crystal structure of Zn2+ bound calprotectin

8SJC の概要

• エントリーDOI: 10.2210/pdb8sjc/pdb
• 分子名称: Protein S100-A8, Protein S100-A9, PENTAETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: metal binding protein, antimicrobial protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46172.20

構造登録者

Perera, Y.R.,Garcia, V.,Guillen, R.M.,Chazin, W.J. (登録日: 2023-04-17, 公開日: 2024-07-03, 最終更新日: 2025-09-24)

主引用文献

Perera, Y.R.,Enriquez, K.T.,Rodriguez, A.,Garcia, V.,Akizuki, T.,Naretto, A.,Togashi, M.,Guillen, R.,Skaar, E.P.,Chazin, W.J.
The C-terminal extension of calprotectin mediates zinc chelation and modulates Staphylococcus aureus biomass accumulation.
Protein Sci., 34:e70294-e70294, 2025

PubMed Abstract: Calprotectin (CP) is an S100A8/S100A9 heterodimer that plays an important role in nutritional immunity at the host-microbe interface. CP combats Staphylococcus aureus growth by sequestration of zinc and other trace transition metals; however, questions remain about whether CP antimicrobial activity strictly relies on metal sequestration. Moreover, the precise mechanism for how zinc binds at the two distinct transition metal binding sites of CP is not known. High-resolution X-ray crystal structures reveal tetracoordinate binding in the canonical HisAsp site and hexacoordinate binding in the His site similar to the binding of manganese and nickel in this site. The S100A9 C-terminal extension (tail) contributes two of the His residues in the His metal-binding site, but measurements of zinc affinity show there is no significant reduction upon mutation of these His residues or deletion of the entire C-terminal tail. Bacterial growth and static biofilm assays show that the His mutations affect S. aureus biomass accumulation differently than loss of the S100A9 C-terminal tail, despite resulting in the same defect in bacterial-CP binding. These results reveal that the S100A9 tail of CP has a role in preventing S. aureus biomass accumulation.

PubMed: 40944454
DOI: 10.1002/pro.70294

実験手法

X-RAY DIFFRACTION (1.87 Å)