PDBsum entry 6drh

Toxin

PDB id: 6drh

Contents

Protein chains

365 a.a.

185 a.a.

Ligands

PO4 ×3

Metals

_MG

Waters ×1705

PDB id:

6drh

Name:

Toxin

Title:

Adp-ribosyltransferase toxin/immunity pair

Structure:

Adp-ribosyl-(dinitrogen reductase) hydrolase. Chain: a, c, e, g. Engineered: yes. Paar repeat-containing protein. Chain: b, d, f, h. Engineered: yes

Source:

Serratia proteamaculans (strain 568). Organism_taxid: 399741. Strain: 568. Gene: spro_3018. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: spro_3017. Expression_system_taxid: 562

Resolution:

2.30Å R-factor: 0.153 R-free: 0.206

Authors:

D.E.Bosch,S.Ting,M.Allaire,J.D.Mougous

Key ref:

S.Y.Ting et al. (2018). Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins. Cell, 175, 1380. PubMed id: 30343895 DOI: 10.1016/j.cell.2018.09.037

Date:

11-Jun-18 Release date: 31-Oct-18

Protein chains

A8GG79  (TRI1_SERP5) -  ADP-ribosylarginine hydrolase Tri1 from Serratia proteamaculans (strain 568)

Seq: 366 a.a.

Struc: 365 a.a.

Protein chains

A8GG78  (TRE1_SERP5) -  NAD(+)--protein-arginine ADP-ribosyltransferase Tre1 from Serratia proteamaculans (strain 568)

Seq: 444 a.a.

Struc: 185 a.a.*

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chains A, C, E, G: E.C.3.2.2.19 - [protein ADP-ribosylarginine] hydrolase.
• Reaction:
  1. N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + H2O = ADP-D-ribose + L-arginyl-[protein]
  2. N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + L-arginine
• Enzyme class 2: Chains B, D, F, H: E.C.2.4.2.31 - NAD(+)--protein-arginine ADP-ribosyltransferase.
• Reaction: L-arginyl-[protein] + NAD⁺ = N(omega)-(ADP-D-ribosyl)-L-arginyl- [protein] + 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.2018.09.037

Cell 175:1380 (2018)

PubMed id: 30343895

Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins.

S.Y.Ting, D.E.Bosch, S.M.Mangiameli, M.C.Radey, S.Huang, Y.J.Park, K.A.Kelly, S.K.Filip, Y.A.Goo, J.K.Eng, M.Allaire, D.Veesler, P.A.Wiggins, S.B.Peterson, J.D.Mougous.

ABSTRACT

ADP-ribosylation of proteins can profoundly impact their function and serves as an effective mechanism by which bacterial toxins impair eukaryotic cell processes. Here, we report the discovery that bacteria also employ ADP-ribosylating toxins against each other during interspecies competition. We demonstrate that one such toxin from Serratia proteamaculans interrupts the division of competing cells by modifying the essential bacterial tubulin-like protein, FtsZ, adjacent to its protomer interface, blocking its capacity to polymerize. The structure of the toxin in complex with its immunity determinant revealed two distinct modes of inhibition: active site occlusion and enzymatic removal of ADP-ribose modifications. We show that each is sufficient to support toxin immunity; however, the latter additionally provides unprecedented broad protection against non-cognate ADP-ribosylating effectors. Our findings reveal how an interbacterial arms race has produced a unique solution for safeguarding the integrity of bacterial cell division machinery against inactivating post-translational modifications.