1K0V

Copper trafficking: the solution structure of Bacillus subtilis CopZ

1K0V の概要

• エントリーDOI: 10.2210/pdb1k0v/pdb
• 関連するPDBエントリー: 1cpz
• NMR情報: BMRB: 5213
• 分子名称: CopZ, COPPER (I) ION (2 entities in total)
• 機能のキーワード: beta-alpha-beta-beta-alpha-beta, metal transport
• 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: 7866.24

構造登録者

Banci, L.,Bertini, I.,Del Conte, R.,Markey, J.,Ruiz-Duenas, F.J. (登録日: 2001-09-21, 公開日: 2001-12-19, 最終更新日: 2024-05-22)

主引用文献

Banci, L.,Bertini, I.,Del Conte, R.,Markey, J.,Ruiz-Duenas, F.J.
Copper trafficking: the solution structure of Bacillus subtilis CopZ.
Biochemistry, 40:15660-15668, 2001

PubMed Abstract: A sequence with a high homology (39% residue identity) with that of the copper-transport CopZ protein from Enterococcus hirae and with the same MXCXXC metal-binding motif has been identified in the genome of Bacillus subtilis, and the corresponding protein has been expressed. The protein, constituted by 73 amino acids, does bind copper(I) under reducing conditions and fully folded in both copper-bound and copper-free forms under the present experimental conditions. The solution structure of the copper-bound form was determined through NMR spectroscopy on an 15N-labeled sample. A total of 1508 meaningful nuclear Overhauser effects, 38 dihedral phi angles, and 48 dihedral psi angles were used in the structural calculations, which lead to a family of 30 conformers with an average rmsd to the mean structure of 0.32 +/- 0.06 A for the backbone and of 0.85 +/- 0.07 A for the heavy atoms. NMR data on the apoprotein also show that, also in this form, the protein is in a folded state and essentially maintains the complete secondary structure. Some disorder is observed in the loop devoted to copper binding. These results are compared with those reported for CopZ from E. hirae whose structure is well-defined only in the apo form. The different behaviors of copper-loaded E. hirae and B. subtilis are tentatively accounted for on the basis of the presence of dithiothreitol used in the latter case, which would stabilize the monomeric form. The comparison is extended to other similar proteins, with particular attention to the copper-binding loop. The nature and the location of conserved residues around the metal-binding site are discussed with respect to their relevance for the metal-binding process. Proposals for the role of CopZ are also presented.

PubMed: 11747441
DOI: 10.1021/bi0112715

実験手法

SOLUTION NMR