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Structure of a conserved hypothetical protein SA1388 from S. aureus reveals a capped hexameric toroid with two PII domain lids and a dinuclear metal center

Authors
Publisher
BioMed Central
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PMC
Keywords
  • Research Article
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  • Biology
  • Chemistry

Abstract

1472-6807-6-27.fm ral ss BioMed CentBMC Structural Biology Open AcceResearch article Structure of a conserved hypothetical protein SA1388 from S. aureus reveals a capped hexameric toroid with two PII domain lids and a dinuclear metal center Kumar Singh Saikatendu1,4, Xuejun Zhang1, Lisa Kinch1,2, Matthew Leybourne3, Nick V Grishin1,2 and Hong Zhang*1 Address: 1Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas TX 75390-8816, USA, 2Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 6001 Forest Park Blvd., Dallas, Texas 75390-9050, USA, 3Department of Geoscience, University of Texas at Dallas, Richardson, Texas 75083-0688, USA and 4Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA, 92037, USA Email: Kumar Singh Saikatendu - [email protected]; Xuejun Zhang - [email protected]; Lisa Kinch - [email protected]; Matthew Leybourne - [email protected]; Nick V Grishin - [email protected]; Hong Zhang* - [email protected] * Corresponding author Abstract Background: The protein encoded by the SA1388 gene from Staphylococcus aureus was chosen for structure determination to elucidate its domain organization and confirm our earlier remote homology based prediction that it housed a nitrogen regulatory PII protein-like domain. SA1388 was predicted to contain a central PII-like domain and two flanking regions, which together belong to the NIF3-like protein family. Proteins like SA1388 remain a poorly studied group and their structural characterization could guide future investigations aimed at understanding their function. Results: The structure of SA1388 has been solved to 2.0Å resolution by single wavelength anomalous dispersion phasing method using selenium anomalous signals. It reveals a canonical NIF3-like fold containing two domains with a PII-like domain inserted in the middle of the polypeptide. The N and C termi

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