9BUJ

Structure of PfPL1 from Pseudoalteromonas fuliginea

Summary for 9BUJ

• Entry DOI: 10.2210/pdb9buj/pdb
• Descriptor: Pectate lyase, CALCIUM ION (3 entities in total)
• Functional Keywords: polysaccharide lyase, pl1, pectin, lyase
• Biological source: Pseudoalteromonas fuliginea
• Total number of polymer chains: 1
• Total formula weight: 51196.23

Authors

Boraston, A.B.,Hobbs, J.K. (deposition date: 2024-05-17, release date: 2024-07-10, Last modification date: 2024-07-17)

Primary citation

Hobbs, J.K.,Boraston, A.B.
The structure of a pectin-active family 1 polysaccharide lyase from the marine bacterium Pseudoalteromonas fuliginea.
Acta Crystallogr.,Sect.F, 80:142-147, 2024

PubMed 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 Ca, 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.

PubMed: 38935515
DOI: 10.1107/S2053230X2400596X

Experimental method

X-RAY DIFFRACTION (2.19 Å)