2ae0
From Proteopedia
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Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold
Overview
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.
About this Structure
2AE0 is a Single protein structure of sequence from Escherichia coli with EDO and ACY as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold., van Straaten KE, Dijkstra BW, Vollmer W, Thunnissen AM, J Mol Biol. 2005 Oct 7;352(5):1068-80. PMID:16139297
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