7P1V

Apo structure of KDNase from Trichophyton Rubrum

7P1V の概要

• エントリーDOI: 10.2210/pdb7p1v/pdb
• 分子名称: Extracellular sialidase/neuraminidase, GLYCEROL, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: carbohydrate metabolism, enzyme structure, protein structure, kdn, kdnase, sialic acid, sialidase, carbohydrate
• 由来する生物種: Trichophyton rubrum (Athlete's foot fungus, Epidermophyton rubrum)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 178775.47

構造登録者

Gloster, T.M.,McMahon, S.A. (登録日: 2021-07-02, 公開日: 2021-10-20, 最終更新日: 2024-01-31)

主引用文献

Nejatie, A.,Steves, E.,Gauthier, N.,Baker, J.,Nesbitt, J.,McMahon, S.A.,Oehler, V.,Thornton, N.J.,Noyovitz, B.,Khazaei, K.,Byers, B.W.,Zandberg, W.F.,Gloster, T.M.,Moore, M.M.,Bennet, A.J.
Kinetic and Structural Characterization of Sialidases (Kdnases) from Ascomycete Fungal Pathogens.
Acs Chem.Biol., 16:2632-2640, 2021

PubMed Abstract: Sialidases catalyze the release of sialic acid from the terminus of glycan chains. We previously characterized the sialidase from the opportunistic fungal pathogen, and showed that it is a Kdnase. That is, this enzyme prefers 3-deoxy-d-glycero-d-galacto-non-2-ulosonates (Kdn glycosides) as the substrate compared to -acetylneuraminides (Neu5Ac). Here, we report characterization and crystal structures of putative sialidases from two other ascomycete fungal pathogens, (S) and (S). Unlike Kdnase (S), hydrolysis with the Neu5Ac substrates was negligible for S and S; thus, S and S are selective Kdnases. The second-order rate constant for hydrolysis of aryl Kdn glycosides by S is similar to that by S but 30-fold higher by S. The structures of these glycoside hydrolase family 33 (GH33) enzymes in complex with a range of ligands for both S and S show subtle changes in ring conformation that mimic the Michaelis complex, transition state, and covalent intermediate formed during catalysis. In addition, they can aid identification of important residues for distinguishing between Kdn and Neu5Ac substrates. When , and were grown in chemically defined media, Kdn was detected in mycelial extracts, but Neu5Ac was only observed in or extracts. The C8 monosaccharide 3-deoxy-d--oct-2-ulosonic acid (Kdo) was also identified in and samples. A fluorescent Kdn probe was synthesized and revealed the localization of S in vesicles at the cell surface.

PubMed: 34724608
DOI: 10.1021/acschembio.1c00666

実験手法

X-RAY DIFFRACTION (1.47 Å)