1rez
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1rez.jpg|left|200px]] | [[Image:1rez.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1rez", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1rez| PDB=1rez | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX''' | '''HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX''' | ||
| Line 30: | Line 27: | ||
[[Category: Sato, K.]] | [[Category: Sato, K.]] | ||
[[Category: Sugita, N.]] | [[Category: Sugita, N.]] | ||
| - | [[Category: | + | [[Category: Glycosydase]] |
| - | [[Category: | + | [[Category: Vertebrate c-type]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:24:54 2008'' | |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:24, 3 May 2008
HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX
Overview
In order to reveal the origin of carbohydrate recognition specificity of human lysozyme by clarifying the difference in the binding mode of ligands in the active site, the inactivation of human lysozyme by 2',3'-epoxypropyl beta-glycoside derivatives of the disaccharides, N,N'-diacetylchitobiose [GlcNAc-beta-(1-->4)-GlcNAc] and N-acetyllactosamine [Gal-beta-(1-->4)-GlcNAc], was investigated and the three-dimensional structures of the affinity-labeled enzymes were determined by X-ray crystallography at 1.7 A resolution. Under the conditions comprising 2.0 x 10(-3) M labeling reagent and 1.0 x 10(-5) M human lysozyme at pH 5.4, 37 degrees C, the reaction time required to reduce the lytic activity against Micrococcus luteus cells to 50% of its initial activity was lengthened by 3.7 times through the substitution of the nonreducing end sugar residue, GlcNAc to Gal. The refined structure of human lysozyme labeled by 2',3'-epoxypropyl beta-glycoside derivatives of N,N'-diacetylchitobiose (HL/NAG-NAG-EPO complex) indicated that the interaction mode of the N,N'-diacetylchitobiose moiety in substites B and C in this study was essentially the same as in the case of the complex of human lysozyme with the free ligand. On the other hand, the hydrogen-bonding pattern and the stacking interaction at subsite B were remarkably different between the HL/NAG-NAG-EPO complex and human lysozyme labeled by the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine (HL/GAL-NAG-EPO complex). The reduced number of possible hydrogen bonds as well as the less favorable stacking between the side chain of Tyr63 in human lysozyme and the galactose residue in the HL/GAL-NAG-EPO complex reasonably explained the less efficient ability of the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine as compared to that of N,N'-diacetylchitobiose as an affinity labeling reagent toward human lysozyme.
About this Structure
1REZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Origin of carbohydrate recognition specificity of human lysozyme revealed by affinity labeling., Muraki M, Harata K, Sugita N, Sato K, Biochemistry. 1996 Oct 22;35(42):13562-7. PMID:8885835 Page seeded by OCA on Sat May 3 07:24:54 2008
