Type III effector NleH2 from Escherichia coli O157:H7 str. Sakai features an atypical protein kinase domain

Andrei S. Halavaty, Spencer M. Anderson, Zdzislaw Wawrzak, Marina Kudritska, Tatiana Skarina, Wayne F. Anderson, Alexei Savchenko*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

The crystal structure of a C-terminal domain of enterohemorrhagic Escherichia coli type III effector NleH2 has been determined to 2.6 Å resolution. The structure resembles those of protein kinases featuring the catalytic, activation, and glycine-rich loop motifs and ATP-binding site. The position of helix αC and the lack of a conserved arginine within an equivalent HRD motif suggested that the NleH2 kinase domain's active conformation might not require phosphorylation. The activation segment markedly contributed to the dimerization interface of NleH2, which can also accommodate the NleH1-NleH2 heterodimer. The C-terminal PDZ-binding motif of NleH2 provided bases for interaction with host proteins.

Original languageEnglish (US)
Pages (from-to)2433-2435
Number of pages3
JournalBiochemistry
Volume53
Issue number15
DOIs
StatePublished - Apr 22 2014

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Type III effector NleH2 from Escherichia coli O157:H7 str. Sakai features an atypical protein kinase domain'. Together they form a unique fingerprint.

Cite this