1d9u
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BACTERIOPHAGE LAMBDA LYSOZYME COMPLEXED WITH A CHITOHEXASACHARIDE
OverviewOverview
The three-dimensional structure of the lytic transglycosylase from, bacteriophage lambda, also known as bacteriophage lambda lysozyme, complexed to the hexasaccharide inhibitor, hexa-N-acetylchitohexaose, has, been determined by X-ray crystallography at 2.6 A resolution. The unit, cell contains two molecules of the lytic transglycosylase with two, hexasaccharides bound. Each enzyme molecule is found to interact with four, N-acetylglucosamine units from one hexasaccharide (subsites A-D) and two, N-acetylglucosamine units from the second hexasaccharide (subsites E and, F), resulting in all six subsites of the active site of this enzyme being, filled. This crystallographic structure, therefore, represents the first, example of a lysozyme in which all subsites are occupied, and detailed, protein-oligosaccharide interactions are now available for this, bacteriophage lytic transglycosylase. Examination of the active site, furthermore reveals that of the two residues that have been implicated in, the reaction mechanism of most other c-type lysozymes (Glu35 and Asp52 in, hen egg white lysozyme), only a homologous Glu residue is present. The, lambda lytic transglycosylase is therefore functionally closely related to, the Escherichia coli Slt70 and Slt35 lytic transglycosylases and goose egg, white lysozyme which also lack the catalytic aspartic acid.
About this StructureAbout this Structure
1D9U is a Single protein structure of sequence from Enterobacteria phage lambda with SO4 as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the lytic transglycosylase from bacteriophage lambda in complex with hexa-N-acetylchitohexaose., Leung AK, Duewel HS, Honek JF, Berghuis AM, Biochemistry. 2001 May 15;40(19):5665-73. PMID:11341831
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