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Article

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

Journal of molecular biology - 7 Oct 2005

van Straaten Karin E, Dijkstra Bauke W, Vollmer Waldemar, Thunnissen Andy-Mark W H

Abstract excerpt

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...

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Source

Identifiers

PMID: 16139297
DOI: 10.1016/j.jmb.2005.07.067

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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