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dc.contributor.authorAlbesa Jové, David
dc.contributor.authorSvetlıkova, Zuzana
dc.contributor.authorTersa Peñacoba, Montserrat
dc.contributor.authorSancho Vaello, Enea
dc.contributor.authorCarreras González, Ana
dc.contributor.authorBonnet, Pascal
dc.contributor.authorArrasate Bermeosolo, Pedro
dc.contributor.authorEguskiza, Ander
dc.contributor.authorAngala, Shiva K.
dc.contributor.authorCifuente, Javier O.
dc.contributor.authorKordulakova, Jana
dc.contributor.authorJackson, Mary
dc.contributor.authorMikusova, Katarına
dc.contributor.authorGuerín, Marcelo Eduardo
dc.date.accessioned2018-02-05T14:17:20Z
dc.date.available2018-02-05T14:17:20Z
dc.date.issued2016-03
dc.identifier.citationNature Communications 7 : (2016) // Article ID 10906es_ES
dc.identifier.issn2041-1723
dc.identifier.urihttp://hdl.handle.net/10810/24827
dc.description.abstractThe biosynthesis of phospholipids and glycolipids are critical pathways for virtually all cell membranes. PatA is an essential membrane associated acyltransferase involved in the biosynthesis of mycobacterial phosphatidyl-myo-inositol mannosides (PIMs). The enzyme transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2. We report here the crystal structures of PatA from Mycobacterium smegmatis in the presence of its naturally occurring acyl donor palmitate and a nonhydrolyzable palmitoyl-CoA analog. The structures reveal an alpha/beta architecture, with the acyl chain deeply buried into a hydrophobic pocket that runs perpendicular to a long groove where the active site is located. Enzyme catalysis is mediated by an unprecedented charge relay system, which markedly diverges from the canonical HX4D motif. Our studies establish the mechanistic basis of substrate/membrane recognition and catalysis for an important family of acyltransferases, providing exciting possibilities for inhibitor design.es_ES
dc.description.sponsorshipThis work was supported by the European Commission Contract HEALTH-F3-2011-260872, the Spanish Ministry of Economy and Competitiveness Contract BIO2013-49022-C2-2-R, and the Basque Government (to M.E.G.); Slovak Research and Development Agency Contract No. DO7RP-0015-11 (to K.M.) and the NIH/NIAID grant AI064798 (to M.J.). D.A.-J. acknowledges the support from Fundacion Biofisica Bizkaia. We gratefully acknowledge Sonia Lopez-Fernandez (Unit of Biophysics, CSIC, UPV/EHU, Spain), Drs E. Ogando and T. Mercero (Scientific Computing Service UPV/EHU, Spain) for technical assistance. We thank the Swiss Light Source (SLS), and the Diamond Light Source (DLS) for granting access to synchrotron radiation facilities and their staff for the onsite assistance. We specially thank the BioStruct-X project to support access to structural biology facilities. We also acknowledge all members of the Structural Glycobiology Group (Spain) for valuable scientific discussions. The following reagent was obtained through BEI Resources, NIAID, NIH: Mycobacterium tuberculosis, Strain H37Rv, Purified Phosphatidylinositol Mannosides 1 and 2 (PIM1,2), NR-14846.es_ES
dc.language.isoenges_ES
dc.publisherNature Publishinges_ES
dc.relationinfo:eu-repo/grantAgreement/MINECO/BIO2013-49022-C2-2-Res_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/*
dc.subjectsquash glycerol-3-phosphate(1)-acyltransferasees_ES
dc.subjectbacillus-calmette-guerines_ES
dc.subjectfatty-acid biosynthesises_ES
dc.subjectphosphatidylinositol mannosideses_ES
dc.subjectmycobacterium phleies_ES
dc.subjectSN-glycerol-3-phosphate acyltransferasees_ES
dc.subjectescherichia-colies_ES
dc.subjectacylation statees_ES
dc.subjectmolecular-basises_ES
dc.subjectmannosyltransferase PimAes_ES
dc.titleStructural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatAes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.holderThis work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/es_ES
dc.rights.holderAtribución 3.0 España
dc.relation.publisherversionhttps://www.nature.com/articles/ncomms10906.pdfes_ES
dc.identifier.doi10.1038/ncomms10906
dc.departamentoesBioquímica y biología moleculares_ES
dc.departamentoeuBiokimika eta biologia molekularraes_ES


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This work is licensed under a Creative Commons Attribution 4.0
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users will need to obtain permission from the license holder to reproduce the material.
To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Except where otherwise noted, this item's license is described as This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/