The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF

Detalhes bibliográficos
Autor(a) principal: Diaz, Z.
Data de Publicação: 2009
Outros Autores: Xavier, KB., Miller, ST.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.7/193
Resumo: Many bacteria produce and respond to the quorum sensing signal autoinducer-2 (AI-2). Escherichia coli and Salmonella typhimurium are among the species with the lsr operon, an operon containing AI-2 transport and processing genes that are up regulated in response to AI-2. One of the Lsr proteins, LsrF, has been implicated in processing the phosphorylated form of AI-2. Here, we present the structure of LsrF, unliganded and in complex with two phospho-AI-2 analogues, ribose-5-phosphate and ribulose-5-phosphate. The crystal structure shows that LsrF is a decamer of (alpha beta)(8)-barrels that exhibit a previously unseen N-terminal domain swap and have high structural homology with aldolases that process phosphorylated sugars. Ligand binding sites and key catalytic residues are structurally conserved, strongly implicating LsrF as a class I aldolase.
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spelling The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrFMany bacteria produce and respond to the quorum sensing signal autoinducer-2 (AI-2). Escherichia coli and Salmonella typhimurium are among the species with the lsr operon, an operon containing AI-2 transport and processing genes that are up regulated in response to AI-2. One of the Lsr proteins, LsrF, has been implicated in processing the phosphorylated form of AI-2. Here, we present the structure of LsrF, unliganded and in complex with two phospho-AI-2 analogues, ribose-5-phosphate and ribulose-5-phosphate. The crystal structure shows that LsrF is a decamer of (alpha beta)(8)-barrels that exhibit a previously unseen N-terminal domain swap and have high structural homology with aldolases that process phosphorylated sugars. Ligand binding sites and key catalytic residues are structurally conserved, strongly implicating LsrF as a class I aldolase.PLOSARCADiaz, Z.Xavier, KB.Miller, ST.2010-08-12T09:08:48Z2009-08-282009-08-28T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.7/193engDiaz, Z., Xavier, KB., Miller, ST. (2009). “The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF”. PLoS Genet. 4 (8): 1-101932-6203info: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:RCAAP2022-11-29T14:34:40Zoai:arca.igc.gulbenkian.pt:10400.7/193Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:11:36.181864Repositório 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 The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
title The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
spellingShingle The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
Diaz, Z.
title_short The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
title_full The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
title_fullStr The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
title_full_unstemmed The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
title_sort The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
author Diaz, Z.
author_facet Diaz, Z.
Xavier, KB.
Miller, ST.
author_role author
author2 Xavier, KB.
Miller, ST.
author2_role author
author
dc.contributor.none.fl_str_mv ARCA
dc.contributor.author.fl_str_mv Diaz, Z.
Xavier, KB.
Miller, ST.
description Many bacteria produce and respond to the quorum sensing signal autoinducer-2 (AI-2). Escherichia coli and Salmonella typhimurium are among the species with the lsr operon, an operon containing AI-2 transport and processing genes that are up regulated in response to AI-2. One of the Lsr proteins, LsrF, has been implicated in processing the phosphorylated form of AI-2. Here, we present the structure of LsrF, unliganded and in complex with two phospho-AI-2 analogues, ribose-5-phosphate and ribulose-5-phosphate. The crystal structure shows that LsrF is a decamer of (alpha beta)(8)-barrels that exhibit a previously unseen N-terminal domain swap and have high structural homology with aldolases that process phosphorylated sugars. Ligand binding sites and key catalytic residues are structurally conserved, strongly implicating LsrF as a class I aldolase.
publishDate 2009
dc.date.none.fl_str_mv 2009-08-28
2009-08-28T00:00:00Z
2010-08-12T09:08:48Z
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/10400.7/193
url http://hdl.handle.net/10400.7/193
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Diaz, Z., Xavier, KB., Miller, ST. (2009). “The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF”. PLoS Genet. 4 (8): 1-10
1932-6203
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.publisher.none.fl_str_mv PLOS
publisher.none.fl_str_mv PLOS
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