PDBsum entry 4zv4

Translation

PDB id: 4zv4

Contents

Protein chains

392 a.a.

162 a.a.

Ligands

GDP ×2

Metals

_MG ×2

PDB id:

4zv4

Name:

Translation

Title:

Structure of tse6 in complex with ef-tu

Structure:

Elongation factor tu. Chain: a, b. Synonym: ef-tu. Engineered: yes. Tse6. Chain: c, d. Fragment: unp residues 265-430. 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: tufa, pa4265, tufb, pa4277. Expressed in: escherichia coli. Expression_system_taxid: 511693. Pseudomonas aeruginosa. Gene: pa0093.

Resolution:

3.50Å R-factor: 0.233 R-free: 0.283

Authors:

J.C.Whitney,S.Sawai,H.Robinson,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 chains

P09591  (EFTU_PSEAE) -  Elongation factor Tu from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 397 a.a.

Struc: 392 a.a.

Protein chains

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: 162 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chains A, B: E.C.3.6.5.3 - protein-synthesizing GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

GTP + H2O = GDP (Bound ligand (Het Group name = GDP) matches with 72.97% similarity) + phosphate + H(+)

• Enzyme class 2: Chains C, D: E.C.3.2.2.5 - NAD(+) glycohydrolase.
• Reaction: NAD⁺ + H2O = ADP-D-ribose + nicotinamide + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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.