4O96

2.60 Angstrom resolution crystal structure of a protein kinase domain of type III effector NleH2 (ECs1814) from Escherichia coli O157:H7 str. Sakai

Summary for 4O96

• Entry DOI: 10.2210/pdb4o96/pdb
• Descriptor: type III effector protein kinase, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: type iii effector protein kinase, nleh2, center for structural genomics of infectious diseases, csgid, niaid, national institute of allergy and infectious diseases, protein kinase fold with n-lobe and c-lobe, hydrolase
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 4
• Total formula weight: 74861.67

Authors

Anderson, S.M.,Halavaty, A.S.,Wawrzak, Z.,Kudritska, M.,Skarina, T.,Yim, V.,Savchenko, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2014-01-01, release date: 2014-01-15, Last modification date: 2024-02-28)

Primary citation

Halavaty, A.S.,Anderson, S.M.,Wawrzak, Z.,Kudritska, M.,Skarina, T.,Anderson, W.F.,Savchenko, A.
Type III Effector NleH2 from Escherichia coli O157:H7 str. Sakai Features an Atypical Protein Kinase Domain.
Biochemistry, 53:2433-2435, 2014

PubMed 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.

PubMed: 24712300
DOI: 10.1021/bi500016j

Experimental method

X-RAY DIFFRACTION (2.6 Å)