3GDF

Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum.

3GDF の概要

• エントリーDOI: 10.2210/pdb3gdf/pdb
• 関連するPDBエントリー: 3GDG
• 分子名称: Probable NADP-dependent mannitol dehydrogenase, ZINC ION (3 entities in total)
• 機能のキーワード: rossmann fold, beta-alpha-beta motifs, open twisted sheet, allergen, nadp, oxidoreductase
• 由来する生物種: Cladosporium herbarum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114249.86

構造登録者

Nuess, D.,Goettig, P.,Magler, I.,Denk, U.,Breitenbach, M.,Schneider, P.B.,Brandstetter, H.,Simon-Nobbe, B. (登録日: 2009-02-24, 公開日: 2010-05-26, 最終更新日: 2023-09-06)

主引用文献

Nuss, D.,Goettig, P.,Magler, I.,Denk, U.,Breitenbach, M.,Schneider, P.B.,Brandstetter, H.,Simon-Nobbe, B.
Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.
Biochimie, 92:985-993, 2010

PubMed Abstract: The ascomycete Cladosporium herbarum is a prominent fungal inducer of Type I allergy. The only major allergen identified so far is Cla h 8, a NADP-dependent mannitol dehydrogenase (MtDH). MtDH, a cytoplasmic protein of 28.5kDa, belongs to the Short chain Dehydrogenases/Reductases (SDR), acting as a NADP-dependent oxidoreductase. In this study, we found that C. herbarum MtDH can exist as monomers, dimers and tetramers in solution and, correspondingly, forms tetramers and higher oligomers in two crystal structures. Additionally, we identified a unique adaptive binding site for the metal ions Na(+) and Zn(2+) that were distinguished by an anomalous dispersion experiment. A Translation-Libration-Screw analysis confirmed the stabilising effect of Zn(2+) for the tetrameric assembly. Moreover, the zinc containing structure explains the mode of MtDH multimerisation by metal bridging of the tetramers. The formation of oligomers and higher multimers of MtDH provides a missing link to its allergenic properties. Based on the well defined active site region and a comparative analysis with related structures, we can also clarify the atypical enzymatic properties of MtDH by two alternative binding modes of the substrate to the active site.

PubMed: 20420880
DOI: 10.1016/j.biochi.2010.04.012

実験手法

X-RAY DIFFRACTION (2.5 Å)