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Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes.

Evrard C, Fastrez J, Declercq JP
J Mol Biol 276 151-64 (1998)
Cited: 35 times
EuropePMC logo PMID: 9514719

Abstract

Like other lysozymes, the bacteriophage lambda lysozyme is involved in the digestion of bacterial walls. This enzyme is remarkable in that its mechanism of action is different from the classical lysozyme's mechanism. From the point of view of protein evolution, it shows features of lysozymes from different classes. The crystal structure of the enzyme in which all tryptophan residues have been replaced by aza-tryptophan has been solved by X-ray crystallography at 2.3 A using a combination of multiple isomorphous replacement, non-crystallographic symmetry averaging and density modification techniques. There are three molecules in the asymmetric unit. The characteristic structural elements of lysozymes are conserved: each molecule is organized in two domains connected by a helix and the essential catalytic residue (Glu19) is located in the depth of a cleft between the two domains. This cleft shows an open conformation in two of the independent molecules, while access to the cavity is much more restricted in the last one. A structural alignment with T4 lysozyme and hen egg white lysozyme allows us to superpose about 60 C alpha atoms with a rms distance close to 2 A. The best alignments concern the helix preceding the catalytic residue, some parts of the beta sheets and the helix joining the two domains. The results of sequence alignments with the V and C lysozymes, in which weak local similarities had been detected, are compared with the structural results.

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  14. Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity. Sagermann M, Matthews BW. J. Mol. Biol. 316 931-940 (2002)
  15. Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme. Evrard C, Fastrez J, Soumillion P. FEBS Lett. 460 442-446 (1999)
  16. Protein crystallization - is it rocket science? DeLucas LJ. Drug Discov. Today 6 734-744 (2001)
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  21. Characterization of the flexible lip regions in bacteriophage lambda lysozyme using MD simulations. Smith LJ, van Gunsteren WF, Hansen N. Eur. Biophys. J. 44 235-247 (2015)
  22. Engineered regulation of lysozyme by the SH3-CB1 binding interaction. Pham E, Truong K. Protein Eng. Des. Sel. 25 307-311 (2012)


Related citations provided by authors (6)

  1. Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans.. Evrard C, Declercq JP, Fastrez J Acta Crystallogr D Biol Crystallogr 53 217-9 (1997)
  2. Phage Lysozymes. Fastrez J Lysozymes: Model Enzymes in Biochemistry and Biology 35- (1996)
  3. Biosynthetic incorporation of 7-azatryptophan into the phage lambda lysozyme: estimation of tryptophan accessibility, effect on enzymatic activity and protein stability.. Soumillion P, Jespers L, Vervoort J, Fastrez J Protein Eng. 8 451-6 (1995)
  4. A large decrease in heat-shock-induced proteolysis after tryptophan starvation leads to increased expression of phage lambda lysozyme cloned in Escherichia coli.. Soumillion P, Fastrez J Biochem. J. 286 ( Pt 1) 187-91 (1992)
  5. Is the Bacteriophage Lambda Lysozyme an Evolutionary Link or a Hybrid between the C and V-Type Lysozymes? Homology Analysis and Detection of the Catalytic Amino Acid Residues. Jespers L, Sonveaux E, Fastrez J J. Mol. Biol. 228 529- (1992)
  6. Overexpression of the phage lambda lysozyme cloned in Escherichia coli: use of a degenerative mixture of synthetic ribosome binding sites and increase of the protein stability in vivo.. Jespers L, Sonveaux E, Fastrez J, Phanapoulos A, Davison J Protein Eng 4 485-92 (1991)

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