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Title: | Structural Studies of the Bacteriophage Lambda Lysozyme Complexed with a Chitohexasaccharide |
Other Titles: | The Structure of λ Lysozyme-Chitohexasaccharide Complex |
Authors: | Leung, Adelaine |
Advisor: | Berghuis, A. M. |
Department: | Biochemistry |
Keywords: | lysozymne;chitohexasaccharide;bacteriophage;structure |
Publication Date: | 1998 |
Abstract: | Lysozyme from the bacteriophage lambda, 1aL, complexed with a chitohexasaccharide has been solved to 2.6 Å by molecular replacement using a mutant form of 1aL as a model. The protein packs as a dimer in the crystal with the backbones of both monomers being nearly identical. The inhibitor molecule resides in the deep cleft in the middle of the bilobal enzyme. Subsites A to Dare occupied by one (GlcNAc)₆ molecule, while the remaining sites interact with two rings from the adjacent (GlcNAc)₆ molecule. The binding mode of 1aL is compared to other lysozymes (HEWL, HuL, GEWL, T4) and Slt70. Interesting differences are noted in the stacking interactions in ring D and the extensive interactions in ring E. It is hypothesized in the thesis that one possible role of the peptide moiety is to interact with Tyr-132, preventing it from forming stacking interactions with ring D, allowing the sugar to penetrate deeper into the active site. Ring E is buried deeply in the enzyme and has a low thermal factor. In addition, the active site is much narrower in 1aL than in other lysozyme structures. A possible explanation has been suggested that rings E and F stay in the active site longer than those in lysozyme to prevent water molecules instead of the O6 atom of ring D to participate in the nucleophilic attack at the end of the reaction. |
URI: | http://hdl.handle.net/11375/22910 |
Appears in Collections: | Digitized Open Access Dissertations and Theses |
Files in This Item:
File | Description | Size | Format | |
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leung_adelaine_k_w_1998_masters.pdf | 14.33 MB | Adobe PDF | View/Open |
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