1S6U

Solution structure and backbone dynamics of the Cu(I) form of the second metal-binding domain of the Menkes protein ATP7A

1S6U の概要

• エントリーDOI: 10.2210/pdb1s6u/pdb
• 関連するPDBエントリー: 1s6o
• NMR情報: BMRB: 6129
• 分子名称: Copper-transporting ATPase 1, COPPER (I) ION (2 entities in total)
• 機能のキーワード: copper homeostasis, metal transport, menkes, structural proteomics in europe, spine, structural genomics, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Isoform 3: Cytoplasm, cytosol (Probable). Isoform 5: Endoplasmic reticulum: Q04656
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8523.53

構造登録者

Banci, L.,Bertini, I.,Del Conte, R.,D'Onofrio, M.,Rosato, A.,Structural Proteomics in Europe (SPINE) (登録日: 2004-01-27, 公開日: 2004-04-06, 最終更新日: 2024-05-22)

主引用文献

Banci, L.,Bertini, I.,Del Conte, R.,D'Onofrio, M.,Rosato, A.
Solution Structure and Backbone Dynamics of the Cu(I) and Apo Forms of the Second Metal-Binding Domain of the Menkes Protein ATP7A.
Biochemistry, 43:3396-3403, 2004

PubMed Abstract: The second domain of the human Menkes protein (MNK2), formed by 72 residues, has been expressed in Escherichia coli, and its structure has been determined by NMR in both the apo and copper-loaded forms. The structures, obtained with (13)C- and (15)N-labeled samples, are of high quality with backbone rmsd values of 0.51 and 0.41 A and CYANA target functions of 0.39 and 0.38 A(2), respectively. The loop involved in copper binding is part of a hydrophobic patch, which is maintained in both forms. Conformational mobility is observed in the apo form in the same loop. A comparison with metallochaperones and soluble domains of P-type ATPases allows us to relate the primary structure to the occurrence of structural rearrangements upon copper binding.

PubMed: 15035611
DOI: 10.1021/bi036042s

実験手法

SOLUTION NMR