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Title
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Crystallization and preliminary X-ray analysis of two variants of the Escherichia coli O157 ParE2-PaaA2 toxin-antitoxin complex
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Author
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Abstract
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| The paaR2-paaA2-parE2 operon is a three-component toxin-antitoxin module encoded in the genome of the human pathogen Escherichia coli O157. The toxin (ParE2) and antitoxin (PaaA2) interact to form a nontoxic toxin-antitoxin complex. In this paper, the crystallization and preliminary characterization of two variants of the ParE2-PaaA2 toxin-antitoxin complex are described. Selenomethionine-derivative crystals of the full-length ParE2-PaaA2 toxin-antitoxin complex diffracted to 2.8 angstrom resolution and belonged to space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 90.5, c = 412.3 angstrom. It was previously reported that the full-length ParE2-PaaA2 toxin-antitoxin complex forms a higher-order oligomer. In contrast, ParE2 and PaaA2(13-63), a truncated form of PaaA2 in which the first 12 N-terminal residues of the antitoxin have been deleted, form a heterodimer as shown by analytical gel filtration, dynamic light scattering and small-angle X-ray scattering. Crystals of the PaaA2(13-63)-ParE2 complex diffracted to 2.7 angstrom resolution and belonged to space group P6(1)22 (or P6(5)22), with unit-cell parameters a = b = 91.6, c = 185.6 angstrom. |
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Language
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English
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Source (journal)
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Acta Chrystallographica Section F. - -
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Publication
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2014
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ISSN
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2053-230X
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DOI
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10.1107/S2053230X1401749X
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Volume/pages
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70
:9
(2014)
, p. 1284-1291
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ISI
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000341818600034
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Full text (Publisher's DOI)
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Full text (publisher's version - intranet only)
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