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Structure of the basal components of a bacterial transporter.(MICROBIOLOGY)(Author abstract)(Report)

Meisner, Jeffrey ; Maehigashi, Tatsuya ; Andre, Ingemar ; Dunham, Christine M. ; Moran, Charles P. , Jr.

Proceedings of the National Academy of Sciences of the United States, April 3, 2012, Vol.109(14), p.5446(6) [Tạp chí có phản biện]

ISSN: 0027-8424

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  • Nhan đề:
    Structure of the basal components of a bacterial transporter.(MICROBIOLOGY)(Author abstract)(Report)
  • Tác giả: Meisner, Jeffrey ; Maehigashi, Tatsuya ; Andre, Ingemar ; Dunham, Christine M. ; Moran, Charles P. , Jr.
  • Chủ đề: Membrane Proteins -- Research
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States, April 3, 2012, Vol.109(14), p.5446(6)
  • Mô tả: Proteins SpollQ and SpolIIAH interact through two membranes to connect the forespore and the mother cell during endospore development in the bacterium Bacillus subtilis. SpolIIAH consists of a transmembrane segment and an extracellular domain with similarity to YscJ proteins. YscJ proteins form large multimeric rings that are the structural scaffolds for the assembly of type III secretion systems in Gram-negative bacteria. The predicted ring-forming motif of SpolIIAH and other evidence Ied to the model that SpollQ and SpolIIAH form the core components of a channel or transporter through which the mother cell nurtures forespore development. Therefore, to understand the roles of SpolllAH and SpollQ in channel formation, it is critical to determine whether SpolIIAH adopts a ring-forming structural motif, and whether interaction of SpolIIAH with SpollQ would preclude ring formation. We report a 2.8-[Angstrom] resolution structure of a complex of SpollQ and SpolIIAH. SpolIIAH folds into the ring-building structural motif, and modeling shows that the structure of the SpolIQ-SpolIIAH complex is compatible with forming a symmetrical oligomer that is similar to those in type III systems. The inner diameters of the two most likely ring models are large enough to accommodate several copies of other integral membrane proteins. SpollQ contains a LytM domain, which is found in metalloendopeptidases, but lacks residues important for metalloprotease activity. Other LytM domains appear to be involved in protein-protein interactions. We found that the LytM domain of SpollQ contains an accessory region that interacts with SpolIIAH. doi/10.1073/pnas.1120113109
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424

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