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Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold

Lookup NU author(s): Professor Waldemar Vollmer


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Lytic transglycosylases are bacterial enzymes involved in the maintenance and growth of the bacterial cell-wall peptidoglycan. They cleave the β-(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 2.0 Å 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 β-barrel fold, similar to that of endoglucanase V from Humicola insolens. The smaller domain also has a β-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.

Publication metadata

Author(s): van Straaten KE, Dijkstra BW, Vollmer W, Thunnissen AMWH

Publication type: Article

Publication status: Published

Journal: Journal of Molecular Biology

Year: 2005

Volume: 352

Issue: 5

Pages: 1068-1080

ISSN (print): 0022-2836

ISSN (electronic): 1089-8638

Publisher: Academic Press


DOI: 10.1016/j.jmb.2005.07.067


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