7OIH

Glycosylation in the crystal structure of neutrophil myeloperoxidase

7OIH の概要

• エントリーDOI: 10.2210/pdb7oih/pdb
• 分子名称: Myeloperoxidase, CHLORIDE ION, CALCIUM ION, ... (17 entities in total)
• 機能のキーワード: peroxidase, microbicidal, hypochlorous acid, glycosylation, paucimannose, hydrid n-glycan, polymorphonuclear leukocytes, dimer, antimicrobial protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 558964.02

構造登録者

Krawczyk, L.,Semwal, S.,Bouckaert, J. (登録日: 2021-05-11, 公開日: 2022-08-24, 最終更新日: 2024-11-06)

主引用文献

Krawczyk, L.,Semwal, S.,Soubhye, J.,Lemri Ouadriri, S.,Prevost, M.,Van Antwerpen, P.,Roos, G.,Bouckaert, J.
Native glycosylation and binding of the antidepressant paroxetine in a low-resolution crystal structure of human myeloperoxidase.
Acta Crystallogr D Struct Biol, 78:1099-1109, 2022

PubMed Abstract: Human myeloperoxidase (MPO) utilizes hydrogen peroxide to oxidize organic compounds and as such plays an essential role in cell-component synthesis, in metabolic and elimination pathways, and in the front-line defence against pathogens. Moreover, MPO is increasingly being reported to play a role in inflammation. The enzymatic activity of MPO has also been shown to depend on its glycosylation. Mammalian MPO crystal structures deposited in the Protein Data Bank (PDB) present only a partial identification of their glycosylation. Here, a newly obtained crystal structure of MPO containing four disulfide-linked dimers and showing an elaborate collection of glycans is reported. These are compared with the glycans identified in proteomics studies and from 18 human MPO structures available in the PDB. The crystal structure also contains bound paroxetine, a blocker of serotonin reuptake that has previously been identified as an irreversible inhibitor of MPO, in the presence of thiocyanate, a physiological substrate of MPO.

PubMed: 36048150
DOI: 10.1107/S2059798322007082

実験手法

X-RAY DIFFRACTION (2.603 Å)