Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli

dc.creatorFerreira, FM
dc.creatorMendoza-Hernandez, G
dc.creatorCastaneda-Bueno, M
dc.creatorAparicio, R
dc.creatorFischer, H
dc.creatorCalcagno, ML
dc.creatorOliva, G
dc.date2006
dc.date37408
dc.date2014-11-19T23:31:28Z
dc.date2015-11-26T17:09:25Z
dc.date2014-11-19T23:31:28Z
dc.date2015-11-26T17:09:25Z
dc.date.accessioned2018-03-28T23:58:03Z
dc.date.available2018-03-28T23:58:03Z
dc.identifierJournal Of Molecular Biology. Academic Press Ltd Elsevier Science Ltd, v. 359, n. 2, n. 308, n. 321, 2006.
dc.identifier0022-2836
dc.identifierWOS:000237908700006
dc.identifier10.1016/j.jmb.2006.03.024
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/79627
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/79627
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/79627
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1280620
dc.descriptionWe report the crystal structure of the apoenzyme of N-acetylglucosamine-6-phosphate (GlcNAc6P) deacetylase from Escherichia coli (EcNAGPase) and the spectrometric evidence of the presence of Zn2+ in the native protein. The GlcNAc6P deacetylase is an enzyme of the amino sugar catabolic pathway that catalyzes the conversion of the GlcNAc6P into glucosamine 6-phosphate (GlcN6P). The crystal structure was phased by the single isomorphous replacement with anomalous scattering (SIRAS) method using low-resolution (2.9 angstrom) iodine anomalous scattering and it was refined against a native dataset up to 2.0 angstrom resolution. The structure is similar to two other NAGPases whose structures are known from Thermotoga maritima (TmNAGPase) and Bacillus subtilis (BsNAGPase); however, it shows a phosphate ion bound at the metal-binding site. Compared to these previous structures, the apoenzyme shows extensive conformational changes in two loops adjacent to the active site. The E. coli enzyme is a tetramer and its dimer-dimer interface was analyzed. The tetrameric structure was confirmed in solution by small-angle X-ray scattering data. Although no metal ions were detected in the present structure, experiments of photon-induced X-ray emission (PIXE) spectra and of inductively coupled plasma emission spectroscopy (ICP-AES) with enzyme that was neither exposed to chelating agents nor metal ions during purification, revealed the presence of 1.4 atoms of Zn per polypeptide chain. Enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations, demonstrate the role of metal ions in EcNAGPase structure and catalysis. (c) 2006 Elsevier Ltd. All rights reserved.
dc.description359
dc.description2
dc.description308
dc.description321
dc.languageen
dc.publisherAcademic Press Ltd Elsevier Science Ltd
dc.publisherLondon
dc.publisherInglaterra
dc.relationJournal Of Molecular Biology
dc.relationJ. Mol. Biol.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectN-acetylglucosamine-6-phosphate deacetylase
dc.subjectamino sugar catabolism
dc.subjectamidohydrolases
dc.subjectPIXE
dc.subjectICP-AES
dc.subjectAcetylglucosamine 6-phosphate Deacetylase
dc.subjectMetallo-beta-lactamase
dc.subjectN-acetylmuramic Acid
dc.subjectCell-wall Murein
dc.subjectGlucosamine-6-phosphate Isomerase
dc.subjectCoordination Geometry
dc.subjectCrystal-structure
dc.subjectMechanism
dc.subjectPurification
dc.subjectDeaminase
dc.titleStructural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli
dc.typeArtículos de revistas


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