Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding

Catabolic ornithine transcarbamylase (cOTC; EC 2.1.3.3) catalyzes the formation of ornithine (ORN) and carbamoyl phosphate from citrulline, which constitutes the second step of the degradation of arginine via the arginine deiminase pathway. Here, we report the crystal structure of cOTC from the lact...

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Detalhes bibliográficos
Autores: De Las Rivas, Blanca, Fox, Gavin C., Martínez-Ripoll, Martín, Rodríguez, Héctor, Muñoz, Rosario, Mancheño, Jose M.
Tipo de documento: artigo
Estado:Versión aceptada para publicación
Data de publicação:2009
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/46877
Acesso em linha:http://hdl.handle.net/10261/46877
Access Level:Acceso aberto
Palavra-chave:Crystal structures
Metal binding
Oligomeric assembly
Ornithine transcarbamylase
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spelling Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-bindingDe Las Rivas, BlancaFox, Gavin C.Martínez-Ripoll, MartínRodríguez, HéctorMuñoz, RosarioMancheño, Jose M.Crystal structuresMetal bindingOligomeric assemblyOrnithine transcarbamylaseCatabolic ornithine transcarbamylase (cOTC; EC 2.1.3.3) catalyzes the formation of ornithine (ORN) and carbamoyl phosphate from citrulline, which constitutes the second step of the degradation of arginine via the arginine deiminase pathway. Here, we report the crystal structure of cOTC from the lactic acid bacteria Lactobacillus hilgardii (Lh-cOTC) refined to 2.1 Å resolution. The structure reveals that Lh-cOTC forms a hexameric assembly, which was also confirmed by gel-filtration chromatography and analytical ultracentrifugation. The homohexamer, with 32 point group symmetry, represents a new oligomeric state within the members of the ornithine transcarbamylase family that are typically homotrimeric or homododecameric. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution. Additionally, the structure reveals, for the first time in the ornithine transcarbamylase family, a metal-binding site located at the 3-fold molecular symmetry axis of each trimerFinancial support from the Ministerio de Educación y Ciencia (BFU2007- 67404/BMC) and the Factoría de Cristalización (Consolider-Ingenio-2007) (to J.M.M.), AGL2008- 001052 (to R.M.), FUN-C-FOOD Consolider 25506 (to R.M.), and Comunidad de Madrid S-0505/AGR/ 000153 (to R.M.) is greatly appreciated. H.R. is a recipient of an I3P predoctoral fellowship from the CSIC. J.M.M. thanks Dr. Shi for kindly providing a sample of PALO.Peer reviewedElsevierMinisterio de Educación y Ciencia (España)Comunidad de MadridMinisterio de Ciencia e Innovación (España)European CommissionConsejo Superior de Investigaciones Científicas (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201220122009info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/46877reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.jmb.2009.08.002Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/468772026-05-22T06:33:51Z
dc.title.none.fl_str_mv Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
title Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
spellingShingle Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
De Las Rivas, Blanca
Crystal structures
Metal binding
Oligomeric assembly
Ornithine transcarbamylase
title_short Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
title_full Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
title_fullStr Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
title_full_unstemmed Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
title_sort Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding
dc.creator.none.fl_str_mv De Las Rivas, Blanca
Fox, Gavin C.
Martínez-Ripoll, Martín
Rodríguez, Héctor
Muñoz, Rosario
Mancheño, Jose M.
author De Las Rivas, Blanca
author_facet De Las Rivas, Blanca
Fox, Gavin C.
Martínez-Ripoll, Martín
Rodríguez, Héctor
Muñoz, Rosario
Mancheño, Jose M.
author_role author
author2 Fox, Gavin C.
Martínez-Ripoll, Martín
Rodríguez, Héctor
Muñoz, Rosario
Mancheño, Jose M.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Educación y Ciencia (España)
Comunidad de Madrid
Ministerio de Ciencia e Innovación (España)
European Commission
Consejo Superior de Investigaciones Científicas (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Crystal structures
Metal binding
Oligomeric assembly
Ornithine transcarbamylase
topic Crystal structures
Metal binding
Oligomeric assembly
Ornithine transcarbamylase
description Catabolic ornithine transcarbamylase (cOTC; EC 2.1.3.3) catalyzes the formation of ornithine (ORN) and carbamoyl phosphate from citrulline, which constitutes the second step of the degradation of arginine via the arginine deiminase pathway. Here, we report the crystal structure of cOTC from the lactic acid bacteria Lactobacillus hilgardii (Lh-cOTC) refined to 2.1 Å resolution. The structure reveals that Lh-cOTC forms a hexameric assembly, which was also confirmed by gel-filtration chromatography and analytical ultracentrifugation. The homohexamer, with 32 point group symmetry, represents a new oligomeric state within the members of the ornithine transcarbamylase family that are typically homotrimeric or homododecameric. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution. Additionally, the structure reveals, for the first time in the ornithine transcarbamylase family, a metal-binding site located at the 3-fold molecular symmetry axis of each trimer
publishDate 2009
dc.date.none.fl_str_mv 2009
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/46877
url http://hdl.handle.net/10261/46877
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.jmb.2009.08.002
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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