Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode
| Main Author: | |
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| Publication Date: | 2012 |
| Other Authors: | , , , , , , , , |
| Format: | Article |
| Language: | eng |
| Source: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
| Download full: | https://doi.org/10.1074/jbc.M112.407700 |
Summary: | PEst-C/EQB/LA0006/2011 This work was supported by Fundação para a Ciência e a Tecnologia Grants PEst-C/EQB/LA0006/2011, PTDC/BIA-PRO/69732/2006, PTDC/QUI-BIQ/100359/2008, and PTDC/BIA-PRO/103980/2008. Supported by Fundação para a Ciência e a Tecnologia individual fellowship SFRH/BD/38667/2007. |
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Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding modeBiochemistryMolecular BiologyCell BiologyPEst-C/EQB/LA0006/2011 This work was supported by Fundação para a Ciência e a Tecnologia Grants PEst-C/EQB/LA0006/2011, PTDC/BIA-PRO/69732/2006, PTDC/QUI-BIQ/100359/2008, and PTDC/BIA-PRO/103980/2008. Supported by Fundação para a Ciência e a Tecnologia individual fellowship SFRH/BD/38667/2007.Protein-protein interactions play a pivotal role in a large number of biological processes exemplified by the assembly of the cellulosome. Integration of cellulosomal components occurs through the binding of type I cohesin modules located in a non-catalytic molecular scaffold to type I dockerin modules located at the C terminus of cellulosomal enzymes. The majority of type I dockerins display internal symmetry reflected by the presence of two essentially identical cohesin-binding surfaces. Here we report the crystal structures of two novel Clostridium thermocellum type I cohesin-dockerin complexes (CohOlpC-Doc124A and CohOlpA-Doc918). The data revealed that the two dockerins, Doc918 and Doc124A, are unusual because they lack the structural symmetry required to support a dual binding mode. Thus, in both cases, cohesin recognition is dominated by residues located at positions 11, 12, and 19 of one of the dockerin binding surfaces. The alternative binding mode is not possible (Doc918) or highly limited (Doc124A) because residues that assume the critical interacting positions, when dockerins are reoriented by 180°, make steric clashes with the cohesin. In common with a third dockerin (Doc258) that also presents a single binding mode, Doc124A directs the appended cellulase, Cel124A, to the surface of C. thermocellum and not to cellulosomes because it binds preferentially to type I cohesins located at the cell envelope. Although there are a few exceptions, such as Doc918 described here, these data suggest that there is considerable selective pressure for the evolution of a dual binding mode in type I dockerins that direct enzymes into cellulosomes.CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)DQ - Departamento de QuímicaRUNBrás, Joana L. A.Alves, Victor D.Carvalho, Ana LuísaNajmudin, ShabirPrates, José A. M.Ferreira, Luís M. A.Bolam, David N.Romão, Maria JoãoGilbert, Harry J.Fontes, Carlos M. G. A.2019-03-11T23:15:06Z2012-12-282012-12-28T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article12application/pdfhttps://doi.org/10.1074/jbc.M112.407700eng0021-9258PURE: 12006540http://www.scopus.com/inward/record.url?scp=84871786607&partnerID=8YFLogxKhttps://doi.org/10.1074/jbc.M112.407700info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-22T17:37:40Zoai:run.unl.pt:10362/62993Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T17:08:36.376464Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse |
| dc.title.none.fl_str_mv |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode |
| title |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode |
| spellingShingle |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode Brás, Joana L. A. Biochemistry Molecular Biology Cell Biology |
| title_short |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode |
| title_full |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode |
| title_fullStr |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode |
| title_full_unstemmed |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode |
| title_sort |
Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode |
| author |
Brás, Joana L. A. |
| author_facet |
Brás, Joana L. A. Alves, Victor D. Carvalho, Ana Luísa Najmudin, Shabir Prates, José A. M. Ferreira, Luís M. A. Bolam, David N. Romão, Maria João Gilbert, Harry J. Fontes, Carlos M. G. A. |
| author_role |
author |
| author2 |
Alves, Victor D. Carvalho, Ana Luísa Najmudin, Shabir Prates, José A. M. Ferreira, Luís M. A. Bolam, David N. Romão, Maria João Gilbert, Harry J. Fontes, Carlos M. G. A. |
| author2_role |
author author author author author author author author author |
| dc.contributor.none.fl_str_mv |
CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE) DQ - Departamento de Química RUN |
| dc.contributor.author.fl_str_mv |
Brás, Joana L. A. Alves, Victor D. Carvalho, Ana Luísa Najmudin, Shabir Prates, José A. M. Ferreira, Luís M. A. Bolam, David N. Romão, Maria João Gilbert, Harry J. Fontes, Carlos M. G. A. |
| dc.subject.por.fl_str_mv |
Biochemistry Molecular Biology Cell Biology |
| topic |
Biochemistry Molecular Biology Cell Biology |
| description |
PEst-C/EQB/LA0006/2011 This work was supported by Fundação para a Ciência e a Tecnologia Grants PEst-C/EQB/LA0006/2011, PTDC/BIA-PRO/69732/2006, PTDC/QUI-BIQ/100359/2008, and PTDC/BIA-PRO/103980/2008. Supported by Fundação para a Ciência e a Tecnologia individual fellowship SFRH/BD/38667/2007. |
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2012 |
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2012-12-28 2012-12-28T00:00:00Z 2019-03-11T23:15:06Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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article |
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publishedVersion |
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https://doi.org/10.1074/jbc.M112.407700 |
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https://doi.org/10.1074/jbc.M112.407700 |
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eng |
| language |
eng |
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0021-9258 PURE: 12006540 http://www.scopus.com/inward/record.url?scp=84871786607&partnerID=8YFLogxK https://doi.org/10.1074/jbc.M112.407700 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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12 application/pdf |
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