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TitleThe molybdenum storage protein forms and deposits distinct polynuclear tungsten oxygen aggregates.
Journal, issue, pagesJ Inorg Biochem, Vol. 234, Page 111904, Year 2022
Publish dateJun 16, 2022
AuthorsIram Aziz / Susann Kaltwasser / Kanwal Kayastha / Radhika Khera / Janet Vonck / Ulrich Ermler /
PubMed AbstractSome N-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, ...Some N-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) 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 WO units at positions exposed to bulk solvent and expanded derivatives with additional WO 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 WO linker. Interestingly, distinct POM cluster structures can originate from identical, highly occupied core fragments of three to seven WO 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.
External linksJ Inorg Biochem / PubMed:35779405
MethodsEM (single particle) / X-ray diffraction
Resolution1.4 - 2.58 Å
Structure data

EMDB-14522, PDB-7z5j:
The molybdenum storage protein loaded with tungstate
Method: EM (single particle) / Resolution: 2.58 Å

PDB-7zqq:
Molybdenum storage protein - LB131H
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-7zr4:
Molybdenum storage protein loaded with polyoxotungstates in the in vivo-like state
Method: X-RAY DIFFRACTION / Resolution: 1.701 Å

PDB-7zse:
Molybdenum storage protein in complex with polyoxotungstates in the in-vitro state
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-MOO:
MOLYBDATE ION

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-IWL:
W11-O35 cluster

ChemComp-IV9:
1,1,3,3,5,7,7,9,11,15,15-undecakis($l^{1}-oxidanyl)-2$l^{4},4$l^{3},6$l^{5},8,10,12,14,16,17,18,19$l^{3},20,21,22,23-pentadecaoxa-1$l^{6},3$l^{6},5$l^{6},7$l^{6},9$l^{6},11$l^{6},13$l^{6},15$l^{6}-octatungstapentadecacyclo[7.7.1.1^{1,13}.1^{3,5}.1^{3,15}.1^{5,7}.1^{5,11}.1^{7,11}.0^{2,13}.0^{2,15}.0^{4,13}.0^{6,9}.0^{6,11}.0^{6,13}.0^{9,19}]tricosane

ChemComp-IWO:
W8-O26 cluster

ChemComp-IWZ:
W10-O37 cluster

ChemComp-IHW:
tungstate cluster

ChemComp-IX3:
W3-O10 cluster


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-CL:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • azotobacter vinelandii dj (bacteria)
  • azotobacter vinelandii (bacteria)
KeywordsMETAL BINDING PROTEIN / Metal storage protein / polytungstate / Keggin ion / EM / polyoxotungstate / metal storage / molybdenum storage / polyoxotungstates / Molybdenum storage protein / polyoxotungstate clusters

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