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PDBsum entry 3gdf
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Oxidoreductase
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PDB id
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3gdf
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the NADP-Dependent mannitol dehydrogenase from cladosporium herbarum: implications for oligomerisation and catalysis.
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Authors
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D.Nüss,
P.Goettig,
I.Magler,
U.Denk,
M.Breitenbach,
P.B.Schneider,
H.Brandstetter,
B.Simon-Nobbe.
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Ref.
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Biochimie, 2010,
92,
985-993.
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PubMed id
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Abstract
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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.
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