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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...

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Autores principales: Geerds, Christina, Haas, Albert, Niemann, Hartmut H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2021
Materias:
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.
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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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