5UJ5

Solution structure of the oxidized iron-sulfur protein adrenodoxin from Encephalitozoon cuniculi. Seattle Structural Genomics Center for Infectious Disease target EncuA.00705.a

Summary for 5UJ5

• Entry DOI: 10.2210/pdb5uj5/pdb
• NMR Information: BMRB: 30231
• Descriptor: Adrenodoxin, FE2/S2 (INORGANIC) CLUSTER (2 entities in total)
• Functional Keywords: infectious diseases, microsporidosis, ssgcid, iron-sulfur protein, structural genomics, seattle structural genomics center for infectious disease, electron transport
• Biological source: Encephalitozoon cuniculi (Microsporidian parasite)
• Total number of polymer chains: 1
• Total formula weight: 14553.31

Authors

Buchko, G.W.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2017-01-17, release date: 2017-02-01, Last modification date: 2024-05-01)

Primary citation

Shaheen, S.,Barrett, K.F.,Subramanian, S.,Arnold, S.L.M.,Laureanti, J.A.,Myler, P.J.,Van Voorhis, W.C.,Buchko, G.W.
Solution structure for an Encephalitozoon cuniculi adrenodoxin-like protein in the oxidized state.
Protein Sci., 29:809-817, 2020

PubMed Abstract: Encephalitozoon cuniculi is a unicellular, obligate intracellular eukaryotic parasite in the Microsporidia family and one of the agents responsible for microsporidosis infections in humans. Like most Microsporidia, the genome of E. cuniculi is markedly reduced and the organism contains mitochondria-like organelles called mitosomes instead of mitochondria. Here we report the solution NMR structure for a protein physically associated with mitosome-like organelles in E. cuniculi, the 128-residue, adrenodoxin-like protein Ec-Adx (UniProt ID Q8SV19) in the [2Fe-2S] ferredoxin superfamily. Oxidized Ec-Adx contains a mixed four-strand β-sheet, β2-β1-β4-β3 (↓↑↑↓), loosely encircled by three α-helices and two 3 -helices. This fold is similar to the structure observed in other adrenodoxin and adrenodoxin-like proteins except for the absence of a fifth anti-parallel β-strand next to β3 and the position of α3. Cross peaks are missing or cannot be unambiguously assigned for 20 amide resonances in the H- N HSQC spectrum of Ec-Adx. These missing residues are clustered primarily in two regions, G48-V61 and L94-L98, containing the four cysteine residues predicted to ligate the paramagnetic [2Fe-2S] cluster. Missing amide resonances in H- N HSQC spectra are detrimental to NMR-based solution structure calculations because H- H NOE restraints are absent (glass half-empty) and this may account for the absent β-strand (β5) and the position of α3 in oxidized Ec-Adx. On the other hand, the missing amide resonances unambiguously identify the presence, and immediate environment, of the paramagnetic [2Fe-2S] cluster in oxidized Ec-Adx (glass half-full).

PubMed: 31912584
DOI: 10.1002/pro.3818

Experimental method

SOLUTION NMR