1EXK

SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.

1EXK の概要

• エントリーDOI: 10.2210/pdb1exk/pdb
• NMR情報: BMRB: 4677
• 分子名称: DNAJ PROTEIN, ZINC ION (2 entities in total)
• 機能のキーワード: extended beta-hairpin, cxxcxgxg, zinc-binding motif, chaperone
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P08622
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8661.52

構造登録者

Martinez-Yamout, M.,Legge, G.B.,Zhang, O.,Wright, P.E.,Dyson, H.J. (登録日: 2000-05-03, 公開日: 2000-07-26, 最終更新日: 2024-05-22)

主引用文献

Martinez-Yamout, M.,Legge, G.B.,Zhang, O.,Wright, P.E.,Dyson, H.J.
Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ.
J.Mol.Biol., 300:805-818, 2000

PubMed Abstract: The solution structure of the cysteine-rich (CR) domain of Escherichia coli DnaJ has been solved by NMR methods. The structure of a 79 residue CR domain construct shows a novel fold with an overall V-shaped extended beta-hairpin topology. The CR domain is characterized by four C-X-X-C-X-G-X-G sequence motifs that bind two zinc ions. Residues in these two zinc modules show strong similarities in the grouping of resonances in the (15)N-(1)H HSQC spectrum and display pseudo-symmetry of the motifs in the calculated structures. The conformation of the cysteine residues coordinated to the zinc ion resembles that of the rubredoxin-knuckle, but there are significant differences in hydrogen bonding patterns in the two motifs. Zinc (15)N-(1)H HSQC titrations indicate that the fold of the isolated DnaJ CR domain is zinc-dependent and that one zinc module folds before the other. The C-X-X-C-X-G-X-G sequence motif is highly conserved in CR domains from a wide variety of species. The three-dimensional structure of the E. coli CR domain indicates that this sequence conservation is likely to result in a conserved structural motif.

PubMed: 10891270
DOI: 10.1006/jmbi.2000.3923

実験手法

SOLUTION NMR