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Publication Abstract from PubMed

Pseudoalteromonas fuliginea sp. PS47 is a recently identified marine bacterium that has extensive enzymatic machinery to metabolize polysaccharides, including a locus that targets pectin-like substrates. This locus contains a gene (locus tag EU509_03255) that encodes a pectin-degrading lyase, called PfPL1, that belongs to polysaccharide lyase family 1 (PL1). The 2.2 A resolution X-ray crystal structure of PfPL1 reveals the compact parallel beta-helix fold of the PL1 family. The back side of the core parallel beta-helix opposite to the active site is a meandering set of five alpha-helices joined by lengthy loops. A comparison of the active site with those of other PL1 enzymes suggests a catalytic mechanism that is independent of metal ions, such as Ca(2+), but that substrate recognition may require metal ions. Overall, this work provides the first structural insight into a pectinase of marine origin and the first structure of a PL1 enzyme in subfamily 2.

The structure of a pectin-active family 1 polysaccharide lyase from the marine bacterium Pseudoalteromonas fuliginea.,Hobbs JK, Boraston AB Acta Crystallogr F Struct Biol Commun. 2024 Jul 1;80(Pt 7):142-147. doi: , 10.1107/S2053230X2400596X. Epub 2024 Jun 27. PMID:38935515^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.