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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
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....
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Academic Press
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896485/ https://www.ncbi.nlm.nih.gov/pubmed/20138150 http://dx.doi.org/10.1016/j.jsb.2010.01.013 |
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author | Shevtsov, Mikhail B. Chen, Yanling Isupov, Michail N. Leech, Andrew Gollnick, Paul Antson, Alfred A. |
author_facet | Shevtsov, Mikhail B. Chen, Yanling Isupov, Michail N. Leech, Andrew Gollnick, Paul Antson, Alfred A. |
author_sort | Shevtsov, Mikhail B. |
collection | PubMed |
description | 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 ∼700 Å(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. |
format | Text |
id | pubmed-2896485 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Academic Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28964852010-08-04 Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers Shevtsov, Mikhail B. Chen, Yanling Isupov, Michail N. Leech, Andrew Gollnick, Paul Antson, Alfred A. J Struct Biol Article 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 ∼700 Å(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. Academic Press 2010-04 /pmc/articles/PMC2896485/ /pubmed/20138150 http://dx.doi.org/10.1016/j.jsb.2010.01.013 Text en © 2010 Elsevier Inc. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license |
spellingShingle | Article Shevtsov, Mikhail B. Chen, Yanling Isupov, Michail N. Leech, Andrew Gollnick, Paul Antson, Alfred A. Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers |
title | Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers |
title_full | Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers |
title_fullStr | Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers |
title_full_unstemmed | Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers |
title_short | Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers |
title_sort | bacillus licheniformis anti-trap can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896485/ https://www.ncbi.nlm.nih.gov/pubmed/20138150 http://dx.doi.org/10.1016/j.jsb.2010.01.013 |
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