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| Identifier |
000337095 |
| Title |
Δομική μελέτη της απακετυλάσης της πεπτιδογλυκάνης BC1960 του Bacillus cereus |
| Alternative Title |
Structural studies of the peptidoglycan deacetylase BC1960 from Bacillus cereus |
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Author
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Τσαλαφούτα, Αλέκα
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Thesis advisor
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Κοκκινίδης, Μιχάλης
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| Abstract |
The bacterial cell wall, which consists mainly of peptidoglycan, plays a vital role in the maintenance of the stability and viability of the bacterial cells. Different kinds of modifications of the peptidoglycan, such as N-acetylglucosamine (GlcNAc) deacetylation, play a crucial role in a number of bacterial biological functions like bacterial growth, cell division and autolysis. Moreover, some microorganisms use peptidoglycan modifications as a means to counteract the activity of the host lysozyme, which suggests a probable biological role of peptidoglycan deacetylases in the protection of bacteria from the defense mechanisms of the host.
The peptidoglycan deacetylase BC1960 from Bacillus cereus is an enzyme that exhibits 94% identity to a polysaccharide deacetylase of Bacillus anthracis. Structural studies of BC1960 have been initiated, not only in order to gain insight into the structural basis of peptidoglycan N-acetylglucosamine deacetylation but also because they may lead to drug design which will be probably also relevant to the homologous enzyme of B. anthracis, a pathogen that is considered as a potential bioweapon.
Crystals of BC1960 were obtained using the hanging-drop vapor diffusion method and a complete data set was collected at 100K to a resolution of 2.38 Å using synchrotron radiation. Processing of the data revealed that the crystals belong to the tetragonal space group P41212 with unit cell parameters a = b = 92.7 Å, c = 242.9 Å and contain 4 monomers in the asymmetric unit.
The BC1960 structure was solved using the Molecular Replacement method and a search model of 27% identity. Structure refinement lead to a model of the BC1960 structure with an Rfactor of 18% and revealed a structurally conserved active site in comparison to other polysaccharide deacetylases. BC1960 is a spherical protein, which adopts an α/β barrel fold with the active site lying in a groove. In the conditions which BC1960 was crystallized, in the active site an acetate molecule is bound making interactions with the highly conserved throughout the CE4 family Zinc-Binding Triad His128-His132-Asp77 and other conserved residues.
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| Language |
Greek |
| Subject |
structure |
| Issue date |
2008-12-04 |
| Collection
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School/Department--School of Sciences and Engineering--Department of Biology--Post-graduate theses
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Type of Work--Post-graduate theses
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| Permanent Link |
https://elocus.lib.uoc.gr//dlib/c/5/9/metadata-dlib-cf652c24679d73971b1f02409ff5c87f_1236754463.tkl
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| Views |
265 |
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