PDBsum entry 1k0s

Signaling protein

PDB id: 1k0s

Contents

Protein chain

151 a.a. *

* Residue conservation analysis

PDB id:

1k0s

Name:

Signaling protein

Title:

Solution structure of the chemotaxis protein chew from the thermophilic organism thermotoga maritima

Structure:

Chemotaxis protein chew. Chain: a. Fragment: chew. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: chew. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

I.J.Griswold,H.Zhou,R.V.Swanson,M.I.Simon,F.W.Dahlquist

Key ref:

I.J.Griswold et al. (2002). The solution structure and interactions of CheW from Thermotoga maritima. Nat Struct Biol, 9, 121-125. PubMed id: 11799399 DOI: 10.1038/nsb753

Date:

20-Sep-01 Release date: 06-Feb-02

Protein chain

Q56311  (CHEW_THEMA) -  Chemotaxis protein CheW from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 151 a.a.

Struc: 151 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nsb753

Nat Struct Biol 9:121-125 (2002)

PubMed id: 11799399

The solution structure and interactions of CheW from Thermotoga maritima.

I.J.Griswold, H.Zhou, M.Matison, R.V.Swanson, L.P.McIntosh, M.I.Simon, F.W.Dahlquist.

ABSTRACT

Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex. The overall fold is similar to the regulatory domain of the chemotaxis kinase CheA. In addition, interactions of CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques. The chemical shift perturbation data show the probable contacts that CheW makes with CheA. In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor. These results provide a structural basis for a model in which CheW acts as a molecular bridge between CheA and the cytoplasmic tails of the receptor.

Selected figure(s)

Figure 2.
Figure 2. Stereo view, topology diagram and superposition of CheA and CheW. a, Stereo view showing the ensemble of NMR-derived structures of CheW, with -strands in red and helices in blue. The 20 lowest energy structures generated with CNS13 are superimposed to the mean. Disordered regions of protein backbone were not used for the superposition. b, Topology diagram of CheW showing the locations of secondary structural elements within the primary sequence. -strands are shown as red arrows; helices, as blue cylinders. c, Ribbon diagram of CheW showing the superposition of the average minimized NMR-derived structure of T. maritima CheW and CheA, using homologous regions of secondary structure. The superposition consists of CheW residues 10 -37, 51 -71, 79 -106, 124 -128 and 121 -141 from CheW (gold) and residues 538 -671 (543 -570, 581 -601, 610 -637, 652 -656 and 660 -670) from CheA (blue). R.m.s. deviation of backbone atoms is 1.95 Å for homologous regions. Residues corresponding to loops 1 and 2 and the C-terminal helix of CheW are colored red. The stereo view and ribbon diagrams were created with MOLMOL31, 32 and RIBBONS33, respectively.

Figure 4.
Figure 4. Ribbon diagrams and molecular surface representations of CheW. a, Ribbon diagrams of the minimized average structure of CheW. The two views are rotated 90° about the x-axis. The order of the secondary structural elements is indicated. Positions of absolutely conserved residues are shown as balls; Gly 51, in red; and Arg 56, Gly 57, Gly 92 and Gly 124, in green. b, Chemical shift perturbations in CheW due to binding of CheA^354 -671, mapped to a molecular surface representation of CheW calculated from its minimized average structure. Color ramp from white to red indicates 0 Hz to 150 Hz change. Gray indicates no available data. c, Location of Tsr repressor mutations (green) mapped onto the surface of CheW. d, Combined map (a + b) of CheA interaction sites and repressor mutations mapped to molecular surface of CheW. Overlap between the two sites is shown in yellow. Surface representations were created with GRASP34, after removal of the N-terminal nine amino acids for clarity.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2002, 9, 121-125) copyright 2002.

Figures were selected by an automated process.