1yrr: Difference between revisions

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[[Image:1yrr.gif|left|200px]]
{{Seed}}
[[Image:1yrr.png|left|200px]]


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{{STRUCTURE_1yrr|  PDB=1yrr  |  SCENE=  }}  
{{STRUCTURE_1yrr|  PDB=1yrr  |  SCENE=  }}  


'''Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution'''
===Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution===




==Overview==
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We 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 A) iodine anomalous scattering and it was refined against a native dataset up to 2.0 A 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.
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{{ABSTRACT_PUBMED_16630633}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli., Ferreira FM, Mendoza-Hernandez G, Castaneda-Bueno M, Aparicio R, Fischer H, Calcagno ML, Oliva G, J Mol Biol. 2006 Jun 2;359(2):308-21. Epub 2006 Mar 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16630633 16630633]
Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli., Ferreira FM, Mendoza-Hernandez G, Castaneda-Bueno M, Aparicio R, Fischer H, Calcagno ML, Oliva G, J Mol Biol. 2006 Jun 2;359(2):308-21. Epub 2006 Mar 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16630633 16630633]
Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli., Ferreira FM, Mendoza-Hernandez G, Calcagno ML, Minauro F, Delboni LF, Oliva G, Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):670-2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10771446 10771446]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: N-acetylglucosamine-6-phosphate deacetylase]]
[[Category: N-acetylglucosamine-6-phosphate deacetylase]]
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[[Category: Oliva, G.]]
[[Category: Oliva, G.]]
[[Category: Beta sandwich]]
[[Category: Beta sandwich]]
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