1. The structure of a pectin‐active family 1 polysaccharide lyase from the marine bacterium Pseudoalteromonas fuliginea.
- Author
-
Hobbs, Joanne K. and Boraston, Alisdair B.
- Subjects
- *
MARINE bacteria , *POLYSACCHARIDES , *PECTINS , *BIOCHEMICAL substrates , *METAL ions , *PECTIC enzymes - Abstract
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 Ca2+, 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. [ABSTRACT FROM AUTHOR]
- Published
- 2024
- Full Text
- View/download PDF