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http://hdl.handle.net/10261/113903
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dc.contributor.author | Artola-Recolons, Cecilia | - |
dc.contributor.author | Bernardo-García, Noelia | - |
dc.contributor.author | Bartual, Sergio G. | - |
dc.contributor.author | Meindl, Kathrin | - |
dc.contributor.author | Usón, Isabel | - |
dc.contributor.author | Hermoso, Juan A. | - |
dc.date.accessioned | 2015-04-21T09:25:56Z | - |
dc.date.available | 2015-04-21T09:25:56Z | - |
dc.date.issued | 2014-07-02 | - |
dc.identifier | doi: 10.1021/cb500439c | - |
dc.identifier | issn: 1554-8937 | - |
dc.identifier.citation | ACS chemical biology 9(9): 2058-2066 (2014) | - |
dc.identifier.uri | http://hdl.handle.net/10261/113903 | - |
dc.description.abstract | © 2014 American Chemical Society. The lytic transglycosylases are essential bacterial enzymes that catalyze the nonhydrolytic cleavage of the glycan strands of the bacterial cell wall. We describe here the structural and catalytic properties of MltC, one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The 2.3 A˚ resolution X-ray structure of a soluble construct of MltC shows a unique, compared to known lytic transglycosylase structures, two-domain structure characterized by an expansive active site of 53 A˚ length extending through an interface between the domains. The structures of three complexes of MltC with cell wall analogues suggest the positioning of the peptidoglycan in the active site both as a substrate and as a product. One complex is suggested to correspond to an intermediate in the course of sequential and exolytic cleavage of the peptidoglycan. Moreover, MltC partitioned its reactive oxocarbenium-like intermediate between trapping by the C6-hydroxyl of the muramyl moiety (lytic transglycosylase activity, the major path) and by water (muramidase activity). Genomic analysis identifies the presence of an MltC homologue in no less than 791 bacterial genomes. While the role of MltC in cell wall assembly and maturation remains uncertain, we propose a functional role for this enzyme as befits the uniqueness of its two-domain structure. (Chemical Equation Presented). | - |
dc.description.sponsorship | This work was supported by a grant from the US National Institutes of Health (GM61629) and by grants BFU2011-25326 (the Spanish Ministry of Economy and Competitiveness) and S2010/BMD-2457 (the Government of Community of Madrid). K.M. is grateful for a Juan de la Cierva grant. I.U. is grateful to the Spanish MINECO and Generalitat de Catalunya for financial support (IDC-20101173 and 2009SGR-1036). The Mass Spectrometry & Proteomics Facility of the University of Notre Dame is supported by grant CHE0741793 from the National Science Foundation | - |
dc.publisher | American Chemical Society | - |
dc.rights | closedAccess | - |
dc.title | Structure and cell wall cleavage by modular lytic transglycosylase MltC of Escherichia coli | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1021/cb500439c | - |
dc.relation.publisherversion | http://dx.doi.org/10.1021/cb500439c | - |
dc.date.updated | 2015-04-21T09:25:56Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.identifier.pmid | 24988330 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
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