PDBsum entry 4zv0

Protein binding

PDB id: 4zv0

Contents

Protein chains

137 a.a.

94 a.a.

Metals

IOD ×10

Waters ×366

PDB id:

4zv0

Name:

Protein binding

Title:

Structure of tse6 in complex with tsi6

Structure:

Antibacterial effector secreted protein (type vi secretion system). Chain: a. Engineered: yes. Tse6-binding/tse6 immunity protein. Chain: b. Engineered: yes

Source:

Pseudomonas aeruginosa (strain atcc 15692 / pao1 / 1c / prs 101 / lmg 12228). Organism_taxid: 208964. Strain: atcc 15692 / pao1 / 1c / prs 101 / lmg 12228. Gene: pa0093. Expressed in: escherichia coli. Expression_system_taxid: 511693. Gene: pa0092.

Resolution:

1.40Å R-factor: 0.147 R-free: 0.164

Authors:

J.C.Whitney,S.Sawai,C.Ralston,J.D.Mougous

Key ref:

J.C.Whitney et al. (2015). An interbacterial NAD(P)(+) glycohydrolase toxin requires elongation factor Tu for delivery to target cells. Cell, 163, 607-619. PubMed id: 26456113 DOI: 10.1016/j.cell.2015.09.027

Date:

18-May-15 Release date: 11-Nov-15

Protein chain

Q9I739  (Q9I739_PSEAE) -  NAD(P)(+) glycohydrolase toxin Tse6 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 430 a.a.

Struc: 137 a.a.

Protein chain

Q9I740  (Q9I740_PSEAE) -  Immune protein Tsi6 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 94 a.a.

Struc: 94 a.a.

Enzyme reactions

• Enzyme class: Chain A: E.C.3.2.2.5 - NAD(+) glycohydrolase.
• Reaction: NAD⁺ + H2O = ADP-D-ribose + nicotinamide + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.cell.2015.09.027

Cell 163:607-619 (2015)

PubMed id: 26456113

An interbacterial NAD(P)(+) glycohydrolase toxin requires elongation factor Tu for delivery to target cells.

J.C.Whitney, D.Quentin, S.Sawai, M.LeRoux, B.N.Harding, H.E.Ledvina, B.Q.Tran, H.Robinson, Y.A.Goo, D.R.Goodlett, S.Raunser, J.D.Mougous.

ABSTRACT

Type VI secretion (T6S) influences the composition of microbial communities by catalyzing the delivery of toxins between adjacent bacterial cells. Here, we demonstrate that a T6S integral membrane toxin from Pseudomonas aeruginosa, Tse6, acts on target cells by degrading the universally essential dinucleotides NAD(+) and NADP(+). Structural analyses of Tse6 show that it resembles mono-ADP-ribosyltransferase proteins, such as diphtheria toxin, with the exception of a unique loop that both excludes proteinaceous ADP-ribose acceptors and contributes to hydrolysis. We find that entry of Tse6 into target cells requires its binding to an essential housekeeping protein, translation elongation factor Tu (EF-Tu). These proteins participate in a larger assembly that additionally directs toxin export and provides chaperone activity. Visualization of this complex by electron microscopy defines the architecture of a toxin-loaded T6S apparatus and provides mechanistic insight into intercellular membrane protein delivery between bacteria.