PDBsum entry 4lrk

Transferase

PDB id: 4lrk

Contents

Protein chains

162 a.a.

Waters ×299

PDB id:

4lrk

Name:

Transferase

Title:

Bacterial effector nleh2 kinase domain

Structure:

Effector nleh2. Chain: a, b, c, d. Fragment: kinase domain (unp residues 140-303). Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83334. Strain: o157:h7 edl933. Gene: ecs1814, nleh2, z6021. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.27Å R-factor: 0.176 R-free: 0.220

Authors:

M.Cygler,A.M.Grishin,Montreal-Kingston Bacterial Structural Genomics Initiative (Bsgi)

Key ref:

A.M.Grishin et al. (2014). NleH defines a new family of bacterial effector kinases. Structure, 22, 250-259. PubMed id: 24373767 DOI: 10.1016/j.str.2013.11.006

Date:

19-Jul-13 Release date: 22-Jan-14

Protein chains

Q8XAL6  (Q8XAL6_ECO57) -  T3SS secreted effector NleH from Escherichia coli O157:H7

Seq: 303 a.a.

Struc: 162 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

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

reference

DOI no: 10.1016/j.str.2013.11.006

Structure 22:250-259 (2014)

PubMed id: 24373767

NleH defines a new family of bacterial effector kinases.

A.M.Grishin, M.Cherney, D.H.Anderson, S.Phanse, M.Babu, M.Cygler.

ABSTRACT

Upon host cell infection, pathogenic Escherichia coli hijacks host cellular processes with the help of 20-60 secreted effector proteins that subvert cellular processes to create an environment conducive to bacterial survival. The NleH effector kinases manipulate the NF-κB pathway and prevent apoptosis. They show low sequence similarity to human regulatory kinases and contain two domains, the N-terminal, likely intrinsically unfolded, and a C-terminal kinase-like domain. We show that these effectors autophosphorylate on sites located predominantly in the N-terminal segment. The kinase domain displays a minimal kinase fold, but lacks an activation loop and the GHI subdomain. Nevertheless, all catalytically important residues are conserved. ATP binding proceeds with minimal structural rearrangements. The NleH structure is the first for the bacterial effector kinases family. NleHs and their homologous effector kinases form a new kinase family within the cluster of eukaryotic-like kinases that includes also Rio, Bud32, and KdoK families.