PDBsum entry 2k77

Chaperone, protein binding

PDB id: 2k77

Contents

Protein chain

145 a.a. *

* Residue conservation analysis

PDB id:

2k77

Name:

Chaperone, protein binding

Title:

Nmr solution structure of the bacillus subtilis clpc n-domain

Structure:

Negative regulator of genetic competence clpc/mecb. Chain: a. Fragment: n-terminal domain (unp residues 1-145). Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Gene: clpc, mecb, bsu00860. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

30 models

Authors:

D.J.Kojetin,P.D.Mclaughlin,R.J.Thompson,M.Rance,J.Cavanagh

Key ref:

D.J.Kojetin et al. (2009). Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions. J Mol Biol, 387, 639-652. PubMed id: 19361434 DOI: 10.1016/j.jmb.2009.01.046

Date:

04-Aug-08 Release date: 28-Apr-09

Protein chain

P37571  (CLPC_BACSU) -  Negative regulator of genetic competence ClpC/MecB from Bacillus subtilis (strain 168)

Seq: 810 a.a.

Struc: 145 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2009.01.046

J Mol Biol 387:639-652 (2009)

PubMed id: 19361434

Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.

D.J.Kojetin, P.D.McLaughlin, R.J.Thompson, D.Dubnau, P.Prepiak, M.Rance, J.Cavanagh.

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.

Selected figure(s)

Figure 1.
Fig. 1. NMR solution structure of N-ClpCR. (a) Stereo backbone trace of the 30 lowest-energy NMR solution structures colored using the chainbow feature of PyMol (N-terminus, blue; C-terminus, red). (b) Cartoon diagram of the 30 lowest-energy NMR solution structures colored using the chainbow feature of PyMol (N-terminus, blue; C-terminus, red). (c) Putty/sausage diagram illustrating regions of structural variation within the NMR ensemble colored using the chainbow feature of PyMol from small (blue) to large (red). (d) Cartoon diagram illustrating the sequentially similar/identical regions and hydrophobic contacts between α2 (red) and α6 (blue), giving rise to a pseudo 2-fold axis of symmetry. Color scheme according to the N-ClpCR repeat sequence in Fig. 2.

Figure 4.
Fig. 4. Structural superposition of N-ClpA, N-ClpB, and N-ClpCR. (a) Ribbon diagram of the ML superposition of N-ClpA, N-ClpB, and N-ClpCR. (b) Putty/sausage diagram illustrating regions of structural variation in the THESEUS ML superposition of N-ClpA, N-ClpB, and N-ClpCR.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2009, 387, 639-652) copyright 2009.

Figures were selected by an automated process.