4LRK

Bacterial Effector NleH2 Kinase Domain

Summary for 4LRK

• Entry DOI: 10.2210/pdb4lrk/pdb
• Related: 4LRJ
• Descriptor: Effector NleH2 (2 entities in total)
• Functional Keywords: structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, kinase fold, bacterial effector kinase, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 74791.59

Authors

Cygler, M.,Grishin, A.M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2013-07-19, release date: 2014-01-22, Last modification date: 2024-02-28)

Primary citation

Grishin, A.M.,Cherney, M.,Anderson, D.H.,Phanse, S.,Babu, M.,Cygler, M.
NleH defines a new family of bacterial effector kinases.
Structure, 22:250-259, 2014

PubMed 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.

PubMed: 24373767
DOI: 10.1016/j.str.2013.11.006

Experimental method

X-RAY DIFFRACTION (2.274 Å)