The structure of a pectin-active family 1 polysaccharide lyase from the marine bacterium Pseudoalteromonas fuliginea.

Autor: Hobbs JK; Department of Biochemistry and Microbiology, University of Victoria, PO Box 1700 STN CSC, Victoria, BC V8W 2Y2, Canada., Boraston AB; Department of Biochemistry and Microbiology, University of Victoria, PO Box 1700 STN CSC, Victoria, BC V8W 2Y2, Canada.
Jazyk: angličtina
Zdroj: Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2024 Jul 01; Vol. 80 (Pt 7), pp. 142-147. Date of Electronic Publication: 2024 Jun 27.
DOI: 10.1107/S2053230X2400596X
Abstrakt: 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 Å resolution X-ray crystal structure of PfPL1 reveals the compact parallel β-helix fold of the PL1 family. The back side of the core parallel β-helix opposite to the active site is a meandering set of five α-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.
(open access.)
Databáze: MEDLINE
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