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Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB
Virulence-associated proteins (Vaps) contribute to the virulence of the pathogen Rhodococcus equi, but their mode of action has remained elusive. All Vaps share a conserved core of about 105 amino acids that folds into a compact eight-stranded antiparallel β-barrel with a unique topology. At the top...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8329714/ https://www.ncbi.nlm.nih.gov/pubmed/34341190 http://dx.doi.org/10.1107/S2053230X2100738X |
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author | Geerds, Christina Haas, Albert Niemann, Hartmut H. |
author_facet | Geerds, Christina Haas, Albert Niemann, Hartmut H. |
author_sort | Geerds, Christina |
collection | PubMed |
description | Virulence-associated proteins (Vaps) contribute to the virulence of the pathogen Rhodococcus equi, but their mode of action has remained elusive. All Vaps share a conserved core of about 105 amino acids that folds into a compact eight-stranded antiparallel β-barrel with a unique topology. At the top of the barrel, four loops connect the eight β-strands. Previous Vap structures did not show concave surfaces that might serve as a ligand-binding site. Here, the structure of VapB in a new crystal form was determined at 1.71 Å resolution. The asymmetric unit contains two molecules. In one of them, the loop regions at the top of the barrel adopt a different conformation from other Vap structures. An outward movement of the loops results in the formation of a hydrophobic cavity that might act as a ligand-binding site. This lends further support to the hypothesis that the structural similarity between Vaps and avidins suggests a potential binding function for Vaps. |
format | Online Article Text |
id | pubmed-8329714 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-83297142021-08-19 Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB Geerds, Christina Haas, Albert Niemann, Hartmut H. Acta Crystallogr F Struct Biol Commun Research Communications Virulence-associated proteins (Vaps) contribute to the virulence of the pathogen Rhodococcus equi, but their mode of action has remained elusive. All Vaps share a conserved core of about 105 amino acids that folds into a compact eight-stranded antiparallel β-barrel with a unique topology. At the top of the barrel, four loops connect the eight β-strands. Previous Vap structures did not show concave surfaces that might serve as a ligand-binding site. Here, the structure of VapB in a new crystal form was determined at 1.71 Å resolution. The asymmetric unit contains two molecules. In one of them, the loop regions at the top of the barrel adopt a different conformation from other Vap structures. An outward movement of the loops results in the formation of a hydrophobic cavity that might act as a ligand-binding site. This lends further support to the hypothesis that the structural similarity between Vaps and avidins suggests a potential binding function for Vaps. International Union of Crystallography 2021-07-28 /pmc/articles/PMC8329714/ /pubmed/34341190 http://dx.doi.org/10.1107/S2053230X2100738X Text en © Christina Geerds et al. 2021 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Research Communications Geerds, Christina Haas, Albert Niemann, Hartmut H. Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB |
title | Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB |
title_full | Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB |
title_fullStr | Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB |
title_full_unstemmed | Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB |
title_short | Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB |
title_sort | conformational changes of loops highlight a potential binding site in rhodococcus equi vapb |
topic | Research Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8329714/ https://www.ncbi.nlm.nih.gov/pubmed/34341190 http://dx.doi.org/10.1107/S2053230X2100738X |
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