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Solution structure for an Encephalitozoon cuniculi adrenodoxin-like protein in the oxidized state

Journal Article · · Protein Science
DOI:https://doi.org/10.1002/pro.3818· OSTI ID:1599908
 [1];  [2];  [3];  [1];  [4];  [5];  [2];  [6]
  1. Univ. of Washington, Seattle, WA (United States). Dept. of Medicine, Division of Allergy and Infectious Disease, Center for Emerging and Remerging Infectious Disease
  2. Univ. of Washington, Seattle, WA (United States). Dept. of Medicine, Division of Allergy and Infectious Disease, Center for Emerging and Remerging Infectious Disease; Seattle Structural Genomics Center for Infectious Diseases (United States)
  3. Seattle Structural Genomics Center for Infectious Diseases (United States); Seattle Children's Research Inst., Seattle, WA (United States). Center for Global Infectious Disease Research
  4. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
  5. Seattle Children's Research Institute (United States); Univ. of Washington, Seattle, WA (United States). Dept. of Medicine, Division of Allergy and Infectious Disease, Center for Emerging and Remerging Infectious Disease; Seattle Structural Genomics Center for Infectious Diseases (United States)
  6. Seattle Structural Genomics Center for Infectious Diseases (United States); Pacific Northwest National Lab. (PNNL), Richland, WA (United States); Univ. of Washington, Seattle, WA (United States)
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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 310-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 1H-15N 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 1H-15N HSQC spectra are detrimental to NMR-based solution structure calculations because 1H-1H 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).
Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Grant/Contract Number:
AC05-76RL01830
OSTI ID:
1599908
Report Number(s):
PNNL-SA-150252
Journal Information:
Protein Science, Journal Name: Protein Science Journal Issue: 3 Vol. 29; ISSN 0961-8368
Publisher:
The Protein SocietyCopyright Statement
Country of Publication:
United States
Language:
English

References (30)

Adrenodoxin: Structure, stability, and electron transfer properties journal January 2000
Adrenodoxin-A versatile ferredoxin journal May 2012
Evaluating protein structures determined by structural genomics consortia journal December 2006
The Tertiary Structure of Full-Length Bovine Adrenodoxin Suggests Functional Dimers journal January 2000
TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts journal June 2009
Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics journal September 2015
Microsporidia: accumulating molecular evidence that a group of amitochondriate and suspectedly primitive eukaryotes are just curious fungi journal April 2000
Highly divergent mitochondrion-related organelles in anaerobic parasitic protozoa journal May 2014
Protein targeting in parasites with cryptic mitochondria journal March 2007
Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis journal December 2016
Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways journal December 2016
A New Electron Transport Mechanism in Mitochondrial Steroid Hydroxylase Systems Based on Structural Changes upon the Reduction of Adrenodoxin † journal June 2002
Refined X-ray Structures of the Oxidized, at 1.3 Å, and Reduced, at 1.17 Å, [2Fe−2S] Ferredoxin from the Cyanobacterium Anabaena PCC7119 Show Redox-Linked Conformational Changes † journal November 1999
Interactions of Human Nucleotide Excision Repair Protein XPA with DNA and RPA70ΔC327:  Chemical Shift Mapping and 15 N NMR Relaxation Studies † journal November 1999
Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi journal November 2001
Deleterious mutation in FDX1L gene is associated with a novel mitochondrial muscle myopathy journal November 2013
Function and biogenesis of iron–sulphur proteins journal August 2009
Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin journal October 2014
An NMR approach to structural proteomics journal February 2002
Microsporidian mitosomes retain elements of the general mitochondrial targeting system journal October 2006
Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis journal June 2010
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment journal June 2002
Distinct Localization Patterns of Two Putative Mitochondrial Proteins in the Microsporidian Encephalitozoon cuniculi journal March 2008
Analysis of the Beta-Tubulin Gene and Morphological Changes of the Microsporidium Anncaliia algerae both Suggest Albendazole Sensitivity journal September 2014
Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures journal August 1997
Zoonotic Potential of the Microsporidia journal July 2005
Tools for integrated sequence-structure analysis with UCSF Chimera journal July 2006
Five Questions about Microsporidia journal September 2009
Therapeutic strategies for human microsporidia infections journal June 2005
Microsporidiosis Acquired Through Solid Organ Transplantation: A Public Health Investigation journal February 2014

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