2K77

NMR solution structure of the Bacillus subtilis ClpC N-domain

2K77 の概要

• エントリーDOI: 10.2210/pdb2k77/pdb
• NMR情報: BMRB: 15910
• 分子名称: Negative regulator of genetic competence clpC/mecB (1 entity in total)
• 機能のキーワード: hsp100/clp/aaa+, n-domain, n-clpcr, chaperone/protease, competence, chaperone, protein binding
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15993.47

構造登録者

Kojetin, D.J.,McLaughlin, P.D.,Thompson, R.J.,Rance, M.,Cavanagh, J. (登録日: 2008-08-04, 公開日: 2009-04-28, 最終更新日: 2024-05-08)

主引用文献

Kojetin, D.J.,McLaughlin, P.D.,Thompson, R.J.,Dubnau, D.,Prepiak, P.,Rance, M.,Cavanagh, J.
Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.
J.Mol.Biol., 387:639-652, 2009

PubMed Abstract: The AAA(+) (ATPases associated with a variety of cellular activities) superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. As part of a large oligomeric complex, ClpC controls an array of cellular processes by recognizing, unfolding, and providing misfolded and aggregated proteins as substrates for the ClpP peptidase. ClpC is unique compared to other HSP100/Clp proteins, as it requires an adaptor protein for all fundamental activities. The NMR solution structure of the N-terminal repeat domain of ClpC (N-ClpCR) comprises two structural repeats of a four-helix motif. NMR experiments used to map the MecA adaptor protein interaction surface of N-ClpCR reveal that regions involved in the interaction possess conformational flexibility and conformational exchange on the microsecond-to-millisecond timescale. The electrostatic surface of N-ClpCR differs substantially from the N-domain of Escherichia coli ClpA and ClpB, suggesting that the electrostatic surface characteristics of HSP100/Clp N-domains may play a role in adaptor protein and substrate interaction specificity, and perhaps contribute to the unique adaptor protein requirement of ClpC.

PubMed: 19361434
DOI: 10.1016/j.jmb.2009.01.046

実験手法

SOLUTION NMR