1P8G

The solution structure of apo CopZ from Bacillus subtilis

1P8G の概要

• エントリーDOI: 10.2210/pdb1p8g/pdb
• 関連するPDBエントリー: 1K0V
• 分子名称: similar to mercuric transport protein (1 entity in total)
• 機能のキーワード: m-x-c-x-x-c motif, beta-alpha-beta-beta-alpha-beta secondary structure, copper chaperone, chaperone
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm: O32221
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7802.69

構造登録者

Banci, L.,Bertini, I.,Del Conte, R. (登録日: 2003-05-07, 公開日: 2003-11-25, 最終更新日: 2024-05-22)

主引用文献

Banci, L.,Bertini, I.,Del Conte, R.
Solution Structure of Apo CopZ from Bacillus subtilis: Further Analysis of the Changes Associated with the Presence of Copper
Biochemistry, 42:13422-13428, 2003

PubMed Abstract: The solution structure of apo CopZ from Bacillus subtilis has been determined with the aim of investigating the changes in the hydrophobic interactions around the M-X-C-X-X-C copper(I) binding motif upon metal binding. The methionine of this motif (Met 11 in CopZ) points toward the solvent in apo CopZ, whereas its sulfur atom is close to the metal ion in the metal-loaded protein, though probably not at binding distance. This change is associated with the weakening of the interaction between Leu 37 and Cys 16, present in the apo form, and the formation of an interaction between Met 11 and Tyr 65. Loops 1, 3, and 5 are affected by metal binding. Comparison with the structure of other homologous proteins confirms that often metal binding affects a hydrophobic patch around the metal site, possibly for optimizing and tuning the hydrophobic interactions with the partners. It is also shown that copper(I) exchanges among apo CopZ molecules in slow exchange on the NMR time scale, whereas it is known that such exchange between partner molecules (i.e., metallochaperones and metal pumps) is fast.

PubMed: 14621987
DOI: 10.1021/bi0353326

実験手法

SOLUTION NMR