5OFZ

PllA lectin, apo

5OFZ の概要

• エントリーDOI: 10.2210/pdb5ofz/pdb
• 分子名称: Uncharacterized protein (2 entities in total)
• 機能のキーワード: plla, apo, lectin, sugar binding protein
• 由来する生物種: Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51878.18

構造登録者

Koehnke, J.,Sikandar, A. (登録日: 2017-07-11, 公開日: 2017-10-04, 最終更新日: 2024-01-17)

主引用文献

Beshr, G.,Sikandar, A.,Jemiller, E.M.,Klymiuk, N.,Hauck, D.,Wagner, S.,Wolf, E.,Koehnke, J.,Titz, A.
Photorhabdus luminescens lectin A (PllA): A new probe for detecting alpha-galactoside-terminating glycoconjugates.
J. Biol. Chem., 292:19935-19951, 2017

PubMed Abstract: Lectins play important roles in infections by pathogenic bacteria, for example, in host colonization, persistence, and biofilm formation. The Gram-negative entomopathogenic bacterium symbiotically lives in insect-infecting nematodes and kills the insect host upon invasion by the nematode. The genome harbors the gene , coding for a novel lectin that we named PllA. We analyzed the binding properties of purified PllA with a glycan array and a binding assay in solution. Both assays revealed a strict specificity of PllA for α-galactoside-terminating glycoconjugates. The crystal structures of apo PllA and complexes with three different ligands revealed the molecular basis for the strict specificity of this lectin. Furthermore, we found that a 90° twist in subunit orientation leads to a peculiar quaternary structure compared with that of its ortholog LecA from We also investigated the utility of PllA as a probe for detecting α-galactosides. The α-Gal epitope is present on wild-type pig cells and is the main reason for hyperacute organ rejection in pig to primate xenotransplantation. We noted that PllA specifically recognizes this epitope on the glycan array and demonstrated that PllA can be used as a fluorescent probe to detect this epitope on primary porcine cells In summary, our biochemical and structural analyses of the lectin PllA have disclosed the structural basis for PllA's high specificity for α-galactoside-containing ligands, and we show that PllA can be used to visualize the α-Gal epitope on porcine tissues.

PubMed: 28972138
DOI: 10.1074/jbc.M117.812792

実験手法

X-RAY DIFFRACTION (1.75 Å)