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  The molybdenum storage protein forms and deposits distinct polynuclear tungsten oxygen aggregates

Aziz, I., Kaltwasser, S., Kayastha, K., Khera, R., Vonck, J., & Ermler, U. (2022). The molybdenum storage protein forms and deposits distinct polynuclear tungsten oxygen aggregates. Journal of Inorganic Biochemistry, 234: 111904. doi:10.1016/j.jinorgbio.2022.111904.

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 Creators:
Aziz, Iram1, Author           
Kaltwasser, Susann2, Author           
Kayastha, Kanwal1, Author           
Khera, Radhika1, Author           
Vonck, Janet3, Author           
Ermler, Ulrich1, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              
3Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: Molybdenum storage protein; Polyoxotungstate cluster; Keggin ion; Assembly mechanism; X-ray structure; Cryo-EM structure
 Abstract: Some N2-fixing bacteria store Mo to maintain the formation of the vital FeMo-cofactor dependent nitrogenase under Mo depleting conditions. The Mo storage protein (MoSto), developed for this purpose, has the unique capability to compactly deposit molybdate as polyoxometalate (POM) clusters in a (αβ)3 hexameric cage; the same occurs with the physicochemically related tungstate. To explore the structural diversity of W-based POM clusters, MoSto loaded under different conditions with tungstate and two site-specifically modified MoSto variants were structurally characterized by X-ray crystallography or single-particle cryo-EM. The MoSto cage contains five major locations for POM clusters occupied among others by heptanuclear, Keggin ion and even Dawson-like species also found in bulk solvent under defined conditions. We found both lacunary derivatives of these archetypical POM clusters with missing WOx units at positions exposed to bulk solvent and expanded derivatives with additional WOx units next to protecting polypeptide segments or other POM clusters. The cryo-EM map, unexpectedly, reveals a POM cluster in the cage center anchored to the wall by a WOx linker. Interestingly, distinct POM cluster structures can originate from identical, highly occupied core fragments of three to seven WOx units that partly correspond to those found in MoSto loaded with molybdate. These core fragments are firmly bound to the complementary protein template in contrast to the more variable, less occupied residual parts of the visible POM clusters. Due to their higher stability, W-based POM clusters are, on average, larger and more diverse than their Mo-based counterparts.

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Language(s): eng - English
 Dates: 2022-06-082022-05-072022-06-122022-06-16
 Publication Status: Published online
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jinorgbio.2022.111904
 Degree: -

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Title: Journal of Inorganic Biochemistry
  Abbreviation : J. Inorg. Biochem.
Source Genre: Journal
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Publ. Info: New York : Elsevier
Pages: - Volume / Issue: 234 Sequence Number: 111904 Start / End Page: - Identifier: ISSN: 0162-0134
CoNE: https://pure.mpg.de/cone/journals/resource/954925478535