PMID:16139297
| Citation |
van Straaten, KE, Dijkstra, BW, Vollmer, W and Thunnissen, AM (2005) Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold. J. Mol. Biol. 352:1068-80 |
|---|---|
| Abstract |
Lytic transglycosylases are bacterial enzymes involved in the maintenance and growth of the bacterial cell-wall peptidoglycan. They cleave the beta-(1,4)-glycosidic bonds in peptidoglycan forming non-reducing 1,6-anhydromuropeptides. The crystal structure of the lytic transglycosylase MltA from Escherichia coli without a membrane anchor was solved at 2.0A resolution. The enzyme has a fold completely different from those of the other known lytic transglycosylases. It contains two domains, the largest of which has a double-psi beta-barrel fold, similar to that of endoglucanase V from Humicola insolens. The smaller domain also has a beta-barrel fold topology, which is weakly related to that of the RNA-binding domain of ribosomal proteins L25 and TL5. A large groove separates the two domains, which can accommodate a glycan strand, as shown by molecular modelling. Several conserved residues, one of which is in a position equivalent to that of the catalytic acid of the H.insolens endoglucanase, flank this putative substrate-binding groove. Mutation of this residue, Asp308, abolished all activity of the enzyme, supporting the direct participation of this residue in catalysis. |
| Links |
PubMed Online version:10.1016/j.jmb.2005.07.067 |
| Keywords |
Amino Acid Sequence; Bacteriolysis/physiology; Binding Sites; Catalytic Domain; Cellulase/genetics; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Glycosyltransferases/chemistry; Glycosyltransferases/genetics; Glycosyltransferases/metabolism; Molecular Sequence Data; Multigene Family; Mutation; Peptidoglycan/metabolism; Plant Proteins/genetics; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology |
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