9lyz
From Proteopedia
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| - | [[Image:9lyz.gif|left|200px]] | + | [[Image:9lyz.gif|left|200px]] |
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| - | '''X-RAY CRYSTALLOGRAPHY OF THE BINDING OF THE BACTERIAL CELL WALL TRISACCHARIDE NAM-NAG-NAM TO LYSOZYME''' | + | {{Structure |
| + | |PDB= 9lyz |SIZE=350|CAPTION= <scene name='initialview01'>9lyz</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY CRYSTALLOGRAPHY OF THE BINDING OF THE BACTERIAL CELL WALL TRISACCHARIDE NAM-NAG-NAM TO LYSOZYME''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 9LYZ is a [ | + | 9LYZ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LYZ OCA]. |
==Reference== | ==Reference== | ||
| - | X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme., Kelly JA, Sielecki AR, Sykes BD, James MN, Phillips DC, Nature. 1979 Dec 20-27;282(5741):875-8. PMID:[http:// | + | X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme., Kelly JA, Sielecki AR, Sykes BD, James MN, Phillips DC, Nature. 1979 Dec 20-27;282(5741):875-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/514367 514367] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: James, M N.G.]] | [[Category: James, M N.G.]] | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:16:39 2008'' |
Revision as of 17:16, 20 March 2008
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X-RAY CRYSTALLOGRAPHY OF THE BINDING OF THE BACTERIAL CELL WALL TRISACCHARIDE NAM-NAG-NAM TO LYSOZYME
Overview
Hen egg white lysozyme was the first enzyme whose structure was determined by X-ray crystallography. The proposed mechanism based on this structure involves the distortion of the saccharide residue (2-acetamido-2-deoxy-D-muramic acid, NAM) in the natural substrate (an alternating beta (1 leads to 4) linked oligomer of 2-acetamido-2-deoxy-D-glucose (NAG) and NAM residues) bound to site D in the binding cleft. The importance of substrate distortion has prompted numerous enzymatic, chemical, theoretical, and physical studies, but there is little direct crystallographic evidence on the conformation of a NAM residue bound at site D. We now present the X-ray structure of the non-hydrolysed trisaccharide NAM-NAG-NAM bound in subsites B, C, D. Our interpretation of the 2.5-A resolution difference map does not involve distortion of this residue in site D. Comparison with the structure of the delta-lactone derived from tetra N-acetylchitotetraose (NAG)3NAL) bound to lysozyme suggests we may be looking at a Michaelis complex.
About this Structure
9LYZ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme., Kelly JA, Sielecki AR, Sykes BD, James MN, Phillips DC, Nature. 1979 Dec 20-27;282(5741):875-8. PMID:514367
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