Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2022 |
| Outros Autores: | , , , , , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| Texto Completo: | http://hdl.handle.net/10362/145601 |
Resumo: | the Associate Laboratory for Animal and Veterinary Sciences (AL4AnimalS) grant LA/P/0059/2020. LA/P/0140/2020 of the Associate Laboratory Institute for Health and Bioeconomy - i4HB. National Institutes of Health R01-GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases. Publisher Copyright: © 2022 The Author(s) |
| id |
RCAP_a4b8581574e9fc5dfa5c50ef3f94988a |
|---|---|
| oai_identifier_str |
oai:run.unl.pt:10362/145601 |
| network_acronym_str |
RCAP |
| network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| repository_id_str |
7160 |
| spelling |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assembliesBiomass degradationCarbohydratesCellulosomeCohesinDockerinProtein complexStructural BiologyBiochemistryMolecular Biologythe Associate Laboratory for Animal and Veterinary Sciences (AL4AnimalS) grant LA/P/0059/2020. LA/P/0140/2020 of the Associate Laboratory Institute for Health and Bioeconomy - i4HB. National Institutes of Health R01-GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases. Publisher Copyright: © 2022 The Author(s)The cellulosome is an elaborate multi-enzyme structure secreted by many anaerobic microorganisms for the efficient degradation of lignocellulosic substrates. It is composed of multiple catalytic and non-catalytic components that are assembled through high-affinity protein-protein interactions between the enzyme-borne dockerin (Doc) modules and the repeated cohesin (Coh) modules present in primary scaffoldins. In some cellulosomes, primary scaffoldins can interact with adaptor and cell-anchoring scaffoldins to create structures of increasing complexity. The cellulosomal system of the ruminal bacterium, Ruminococcus flavefaciens, is one of the most intricate described to date. An unprecedent number of different Doc specificities results in an elaborate architecture, assembled exclusively through single-binding-mode type-III Coh-Doc interactions. However, a set of type-III Docs exhibits certain features associated with the classic dual-binding mode Coh-Doc interaction. Here, the structure of the adaptor scaffoldin-borne ScaH Doc in complex with the Coh from anchoring scaffoldin ScaE is described. This complex, unlike previously described type-III interactions in R. flavefaciens, was found to interact in a dual-binding mode. The key residues determining Coh recognition were also identified. This information was used to perform structure-informed protein engineering to change the electrostatic profile of the binding surface and to improve the affinity between the two modules. The results show that the nature of the residues in the ligand-binding surface plays a major role in Coh recognition and that Coh-Doc affinity can be manipulated through rational design, a key feature for the creation of designer cellulosomes or other affinity-based technologies using tailored Coh-Doc interactions.UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNDuarte, MarleneAlves, Victor D.Correia, MárciaCaseiro, CatarinaFerreira, Luís M. A.Romão, Maria JoãoCarvalho, Ana LuísaNajmudin, ShabirBayer, Edward A.Fontes, Carlos M. G. A.Bule, Pedro2022-11-17T22:13:26Z2023-01-012023-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article13application/pdfhttp://hdl.handle.net/10362/145601eng0141-8130PURE: 47766235https://doi.org/10.1016/j.ijbiomac.2022.10.102info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T05:26:08Zoai:run.unl.pt:10362/145601Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:52:10.253409Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
| dc.title.none.fl_str_mv |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies |
| title |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies |
| spellingShingle |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies Duarte, Marlene Biomass degradation Carbohydrates Cellulosome Cohesin Dockerin Protein complex Structural Biology Biochemistry Molecular Biology |
| title_short |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies |
| title_full |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies |
| title_fullStr |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies |
| title_full_unstemmed |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies |
| title_sort |
Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies |
| author |
Duarte, Marlene |
| author_facet |
Duarte, Marlene Alves, Victor D. Correia, Márcia Caseiro, Catarina Ferreira, Luís M. A. Romão, Maria João Carvalho, Ana Luísa Najmudin, Shabir Bayer, Edward A. Fontes, Carlos M. G. A. Bule, Pedro |
| author_role |
author |
| author2 |
Alves, Victor D. Correia, Márcia Caseiro, Catarina Ferreira, Luís M. A. Romão, Maria João Carvalho, Ana Luísa Najmudin, Shabir Bayer, Edward A. Fontes, Carlos M. G. A. Bule, Pedro |
| author2_role |
author author author author author author author author author author |
| dc.contributor.none.fl_str_mv |
UCIBIO - Applied Molecular Biosciences Unit DQ - Departamento de Química RUN |
| dc.contributor.author.fl_str_mv |
Duarte, Marlene Alves, Victor D. Correia, Márcia Caseiro, Catarina Ferreira, Luís M. A. Romão, Maria João Carvalho, Ana Luísa Najmudin, Shabir Bayer, Edward A. Fontes, Carlos M. G. A. Bule, Pedro |
| dc.subject.por.fl_str_mv |
Biomass degradation Carbohydrates Cellulosome Cohesin Dockerin Protein complex Structural Biology Biochemistry Molecular Biology |
| topic |
Biomass degradation Carbohydrates Cellulosome Cohesin Dockerin Protein complex Structural Biology Biochemistry Molecular Biology |
| description |
the Associate Laboratory for Animal and Veterinary Sciences (AL4AnimalS) grant LA/P/0059/2020. LA/P/0140/2020 of the Associate Laboratory Institute for Health and Bioeconomy - i4HB. National Institutes of Health R01-GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases. Publisher Copyright: © 2022 The Author(s) |
| publishDate |
2022 |
| dc.date.none.fl_str_mv |
2022-11-17T22:13:26Z 2023-01-01 2023-01-01T00:00:00Z |
| dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
| dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/145601 |
| url |
http://hdl.handle.net/10362/145601 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
0141-8130 PURE: 47766235 https://doi.org/10.1016/j.ijbiomac.2022.10.102 |
| dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
13 application/pdf |
| dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
| instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
| instacron_str |
RCAAP |
| institution |
RCAAP |
| reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
| repository.mail.fl_str_mv |
|
| _version_ |
1799138113553956864 |