6ITG

a new alginate lyase (PL6) from Vibrio splendidus OU02

Summary for 6ITG

• Entry DOI: 10.2210/pdb6itg/pdb
• Descriptor: Alginate lyase, GLYCEROL, MALONATE ION, ... (4 entities in total)
• Functional Keywords: lyase
• Biological source: Vibrio splendidus
• Total number of polymer chains: 2
• Total formula weight: 118641.95

Authors

Liu, W.Z.,Lyu, Q.Q. (deposition date: 2018-11-23, release date: 2019-05-01, Last modification date: 2023-11-22)

Primary citation

Lyu, Q.,Zhang, K.,Shi, Y.,Li, W.,Diao, X.,Liu, W.
Structural insights into a novel Ca2+-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution.
Biochim Biophys Acta Gen Subj, 1863:1167-1176, 2019

PubMed Abstract: Alginate lyases have a wide range of industrial applications, such as oligosaccharide preparation, medical treatment, and bioconversion. Therefore, the discovery and characterization of novel alginate lyases are extremely important. PL-6 alginate lyases are classified into two groups: those with a single domain or two domains. However, only one structure of a two-domain alginate lyase has been determined to date. In this study, we characterized a novel single-domain PL-6 alginate lyase (named AlyF). According to the biochemical analysis, AlyF possesses unique features compared with other PL-6 enzymes, including (1) a Ca-independent catalytic mechanism and (2) a PolyG-specific cleavage specificity that predominantly produces trisaccharides. The structures of AlyF and its complexes described here reveal the structural basis for these unique features and substrate binding mechanisms, which were further confirmed using mutagenesis. More importantly, we determined the possible subsites specifying the predominantly trisaccharide products of AlyF, which may facilitate the rational design of AlyF for potential applications in preparing a single alginate oligomer.

PubMed: 31004719
DOI: 10.1016/j.bbagen.2019.04.013

Experimental method

X-RAY DIFFRACTION (1.42 Å)