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

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Halavaty AS,Anderson SM,Wawrzak Z,Kudritska M,Skarina T,Anderson WF,Savchenko A

doi

10.1021/bi500016j

subject

Has Abstract

pub_date

2014-04-22 00:00:00

pages

2433-5

issue

15

eissn

0006-2960

issn

1520-4995

journal_volume

53

pub_type

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