PDBsum entry 2kmt

Toxin

PDB id

2kmt

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Contents

			Protein chains

					105 a.a. *

* Residue conservation analysis

PDB id:

2kmt

Links
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Name:

Toxin

Title:

Nmr solution structure of vibrio fischeri ccdb

Structure:

Ccdb. Chain: a, b. Engineered: yes

Source:

Vibrio fischeri. Organism_taxid: 668. Gene: ccdb. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

K.Zangger

Key ref:

N.De Jonge et al. (2010). Structural and thermodynamic characterization of Vibrio fischeri CcdB. J Biol Chem, 285, 5606-5613. PubMed id: 19959472

Date:

04-Aug-09

Release date:

01-Dec-09

PROCHECK

	Headers

	References

Protein chains

Q84B82 (Q84B82_ALIFS) - Toxin CcdB from Aliivibrio fischeri

Seq: Struc:					105 a.a. 105 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	J Biol Chem 285:5606-5613 (2010)
PubMed id: 19959472

Structural and thermodynamic characterization of Vibrio fischeri CcdB.
N.De Jonge, W.Hohlweg, A.Garcia-Pino, M.Respondek, L.Buts, S.Haesaerts, J.Lah, K.Zangger, R.Loris.

ABSTRACT

CcdB(Vfi) from Vibrio fischeri is a member of the CcdB family of toxins that poison covalent gyrase-DNA complexes. In solution CcdB(Vfi) is a dimer that unfolds to the corresponding monomeric components in a two-state fashion. In the unfolded state, the monomer retains a partial secondary structure. This observation correlates well with the crystal and NMR structures of the protein, which show a dimer with a hydrophobic core crossing the dimer interface. In contrast to its F plasmid homologue, CcdB(Vfi) possesses a rigid dimer interface, and the apparent relative rotations of the two subunits are due to structural plasticity of the monomer. CcdB(Vfi) shows a number of non-conservative substitutions compared with the F plasmid protein in both the CcdA and the gyrase binding sites. Although variation in the CcdA interaction site likely determines toxin-antitoxin specificity, substitutions in the gyrase-interacting region may have more profound functional implications.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21315267

T.R.Blower, G.P.Salmond, and B.F.Luisi (2011).
Balancing at survival's edge: the structure and adaptive benefits of prokaryotic toxin-antitoxin partners.

Curr Opin Struct Biol, 21, 109-118.

20677831

C.Göbl, S.Kosol, T.Stockner, H.M.Rückert, and K.Zangger (2010).
Solution structure and membrane binding of the toxin fst of the par addiction module.

Biochemistry, 49, 6567-6575.

PDB code:

2kv5

20952390

J.Yuan, Y.Sterckx, L.A.Mitchenall, A.Maxwell, R.Loris, and M.K.Waldor (2010).
Vibrio cholerae ParE2 poisons DNA gyrase via a mechanism distinct from other gyrase inhibitors.

J Biol Chem, 285, 40397-40408.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.