Cargando…
Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites
The members of the avidin protein family are well known for their high affinity towards d-biotin and their structural stability. These properties make avidins a valuable tool for various biotechnological applications. In the present study, two avidin-like biotin-binding proteins (named streptavidin...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7924230/ https://www.ncbi.nlm.nih.gov/pubmed/33708394 http://dx.doi.org/10.1107/S2052252520015675 |
_version_ | 1783659047379009536 |
---|---|
author | Jeon, Byeong Jun Kim, Sulhee Kim, Min-Seok Lee, Ji-Ho Kim, Beom Seok Hwang, Kwang Yeon |
author_facet | Jeon, Byeong Jun Kim, Sulhee Kim, Min-Seok Lee, Ji-Ho Kim, Beom Seok Hwang, Kwang Yeon |
author_sort | Jeon, Byeong Jun |
collection | PubMed |
description | The members of the avidin protein family are well known for their high affinity towards d-biotin and their structural stability. These properties make avidins a valuable tool for various biotechnological applications. In the present study, two avidin-like biotin-binding proteins (named streptavidin C1 and C2) from Streptomyces cinnamonensis were newly identified while exploring antifungal proteins against Fusarium oxysporum f. sp. cucumerinum. Streptavidin C1 reveals a low correlation (a sequence identity of approximately 64%) with all known streptavidins, whereas streptavidin C2 shares a sequence identity of approximately 94% with other streptavidins. Here, the crystal structures of streptavidin C1 in the mature form and in complex with biotin at 2.1 and 2.5 Å resolution, respectively, were assessed. The overall structures present similar tetrameric features with D (2) symmetry to other (strept)avidin structures. Interestingly, the long C-terminal region comprises a short α-helix (C-Lid; residues 169–179) and an extension C-terminal peptide (ECP; residues 180–191) which stretches into the biotin-binding sites of the same monomer. This ECP sequence (–(180)VTSANPPAS(188)–) is a newly defined biotin-binding site, which reduces the ability to bind to (strept)avidin family proteins. The novel streptavidin C1 could help in the development of an engineered tetrameric streptavidin with reduced biotin-binding capacity as well as other biomaterial tools. |
format | Online Article Text |
id | pubmed-7924230 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-79242302021-03-10 Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites Jeon, Byeong Jun Kim, Sulhee Kim, Min-Seok Lee, Ji-Ho Kim, Beom Seok Hwang, Kwang Yeon IUCrJ Research Papers The members of the avidin protein family are well known for their high affinity towards d-biotin and their structural stability. These properties make avidins a valuable tool for various biotechnological applications. In the present study, two avidin-like biotin-binding proteins (named streptavidin C1 and C2) from Streptomyces cinnamonensis were newly identified while exploring antifungal proteins against Fusarium oxysporum f. sp. cucumerinum. Streptavidin C1 reveals a low correlation (a sequence identity of approximately 64%) with all known streptavidins, whereas streptavidin C2 shares a sequence identity of approximately 94% with other streptavidins. Here, the crystal structures of streptavidin C1 in the mature form and in complex with biotin at 2.1 and 2.5 Å resolution, respectively, were assessed. The overall structures present similar tetrameric features with D (2) symmetry to other (strept)avidin structures. Interestingly, the long C-terminal region comprises a short α-helix (C-Lid; residues 169–179) and an extension C-terminal peptide (ECP; residues 180–191) which stretches into the biotin-binding sites of the same monomer. This ECP sequence (–(180)VTSANPPAS(188)–) is a newly defined biotin-binding site, which reduces the ability to bind to (strept)avidin family proteins. The novel streptavidin C1 could help in the development of an engineered tetrameric streptavidin with reduced biotin-binding capacity as well as other biomaterial tools. International Union of Crystallography 2021-01-11 /pmc/articles/PMC7924230/ /pubmed/33708394 http://dx.doi.org/10.1107/S2052252520015675 Text en © Byeong Jun Jeon et al. 2021 http://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.http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Research Papers Jeon, Byeong Jun Kim, Sulhee Kim, Min-Seok Lee, Ji-Ho Kim, Beom Seok Hwang, Kwang Yeon Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites |
title | Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites |
title_full | Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites |
title_fullStr | Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites |
title_full_unstemmed | Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites |
title_short | Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites |
title_sort | insights into the structure of mature streptavidin c1 from streptomyces cinnamonensis reveal the self-binding of the extension c-terminal peptide to biotin-binding sites |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7924230/ https://www.ncbi.nlm.nih.gov/pubmed/33708394 http://dx.doi.org/10.1107/S2052252520015675 |
work_keys_str_mv | AT jeonbyeongjun insightsintothestructureofmaturestreptavidinc1fromstreptomycescinnamonensisrevealtheselfbindingoftheextensioncterminalpeptidetobiotinbindingsites AT kimsulhee insightsintothestructureofmaturestreptavidinc1fromstreptomycescinnamonensisrevealtheselfbindingoftheextensioncterminalpeptidetobiotinbindingsites AT kimminseok insightsintothestructureofmaturestreptavidinc1fromstreptomycescinnamonensisrevealtheselfbindingoftheextensioncterminalpeptidetobiotinbindingsites AT leejiho insightsintothestructureofmaturestreptavidinc1fromstreptomycescinnamonensisrevealtheselfbindingoftheextensioncterminalpeptidetobiotinbindingsites AT kimbeomseok insightsintothestructureofmaturestreptavidinc1fromstreptomycescinnamonensisrevealtheselfbindingoftheextensioncterminalpeptidetobiotinbindingsites AT hwangkwangyeon insightsintothestructureofmaturestreptavidinc1fromstreptomycescinnamonensisrevealtheselfbindingoftheextensioncterminalpeptidetobiotinbindingsites |