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
Biochemistryjournal_title
Biochemistryauthors
Halavaty AS,Anderson SM,Wawrzak Z,Kudritska M,Skarina T,Anderson WF,Savchenko Adoi
10.1021/bi500016jsubject
Has Abstractpub_date
2014-04-22 00:00:00pages
2433-5issue
15eissn
0006-2960issn
1520-4995journal_volume
53pub_type
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