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2INW

Crystal structure of Q83JN9 from Shigella flexneri at high resolution. Northeast Structural Genomics Consortium target SfR137.

Summary for 2INW
Entry DOI10.2210/pdb2inw/pdb
Related2H28
DescriptorPutative structural protein, PHOSPHATE ION (3 entities in total)
Functional Keywordsq83jn9 x-ray nesg sfr137, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, unknown function
Biological sourceShigella flexneri
Total number of polymer chains2
Total formula weight30007.74
Authors
Primary citationArbing, M.A.,Handelman, S.K.,Kuzin, A.P.,Verdon, G.,Wang, C.,Su, M.,Rothenbacher, F.P.,Abashidze, M.,Liu, M.,Hurley, J.M.,Xiao, R.,Acton, T.,Inouye, M.,Montelione, G.T.,Woychik, N.A.,Hunt, J.F.
Crystal Structures of Phd-Doc, HigA, and YeeU Establish Multiple Evolutionary Links between Microbial Growth-Regulating Toxin-Antitoxin Systems.
Structure, 18:996-1010, 2010
Cited by
PubMed Abstract: Bacterial toxin-antitoxin (TA) systems serve a variety of physiological functions including regulation of cell growth and maintenance of foreign genetic elements. Sequence analyses suggest that TA families are linked by complex evolutionary relationships reflecting likely swapping of functional domains between different TA families. Our crystal structures of Phd-Doc from bacteriophage P1, the HigA antitoxin from Escherichia coli CFT073, and YeeU of the YeeUWV systems from E. coli K12 and Shigella flexneri confirm this inference and reveal additional, unanticipated structural relationships. The growth-regulating Doc toxin exhibits structural similarity to secreted virulence factors that are toxic for eukaryotic target cells. The Phd antitoxin possesses the same fold as both the YefM and NE2111 antitoxins that inhibit structurally unrelated toxins. YeeU, which has an antitoxin-like activity that represses toxin expression, is structurally similar to the ribosome-interacting toxins YoeB and RelE. These observations suggest extensive functional exchanges have occurred between TA systems during bacterial evolution.
PubMed: 20696400
DOI: 10.1016/j.str.2010.04.018
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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