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Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers.

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Shevtsov MB, Chen Y, Isupov MN, Leech A, Gollnick P, Antson AA
OpenAccess logo J Struct Biol 170 127-33 (2010)
Cited: 3 times
EuropePMC logo PMID: 20138150

Abstract

Anti-TRAP (AT) protein regulates expression of tryptophan biosynthetic genes by binding to the trp RNA-binding attenuation protein (TRAP) and preventing its interaction with RNA. Bacillus subtilis AT forms trimers that can either interact with TRAP or can further assemble into dodecameric particles. To determine which oligomeric forms are preserved in AT proteins of other Bacilli we studied Bacillus licheniformis AT which shares 66% sequence identity with the B. subtilis protein. We show that in solution B. licheniformis AT forms stable trimers. In crystals, depending on pH, such trimers assemble into two different types of dodecameric particles, both having 23 point group symmetry. The dodecamer formed at pH 6.0 has the same conformation as previously observed for B. subtilis AT. This dodecamer contains a large internal chamber with the volume of approximately 700 A(3), which is lined by the side chains of twelve valine residues. The presence of the hydrophobic chamber hints at the possibility that the dodecamer formation could be induced by binding of a ligand. Interestingly, in the dodecamer formed at pH 8.0 all trimers are turned inside out relatively to the form observed at pH 6.0.

Articles - 3ld0 mentioned but not cited (1)

  1. Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers. Shevtsov MB, Chen Y, Isupov MN, Leech A, Gollnick P, Antson AA. J Struct Biol 170 127-133 (2010)


Articles citing this publication (2)

  1. Space-group and origin ambiguity in macromolecular structures with pseudo-symmetry and its treatment with the program Zanuda. Lebedev AA, Isupov MN. Acta Crystallogr D Biol Crystallogr 70 2430-2443 (2014)
  2. Mechanism for pH-dependent gene regulation by amino-terminus-mediated homooligomerization of Bacillus subtilis anti-trp RNA-binding attenuation protein. Sachleben JR, McElroy CA, Gollnick P, Foster MP. Proc Natl Acad Sci U S A 107 15385-15390 (2010)


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