3UEP
Crystal structure of YscQ-C from Yersinia pseudotuberculosis
3UEP の概要
| エントリーDOI | 10.2210/pdb3uep/pdb |
| 分子名称 | YscQ-C, type III secretion protein (2 entities in total) |
| 機能のキーワード | type iii secretion protein, cytosol, protein transport |
| 由来する生物種 | Yersinia pseudotuberculosis |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 21404.27 |
| 構造登録者 | |
| 主引用文献 | Bzymek, K.P.,Hamaoka, B.Y.,Ghosh, P. Two Translation Products of Yersinia yscQ Assemble To Form a Complex Essential to Type III Secretion. Biochemistry, 51:1669-1677, 2012 Cited by PubMed Abstract: The bacterial flagellar C-ring is composed of two essential proteins, FliM and FliN. The smaller protein, FliN, is similar to the C-terminus of the larger protein, FliM, both being composed of SpoA domains. While bacterial type III secretion (T3S) systems encode many proteins in common with the flagellum, they mostly have a single protein in place of FliM and FliN. This protein resembles FliM at its N-terminus and is as large as FliM but is more like FliN at its C-terminal SpoA domain. We have discovered that a FliN-sized cognate indeed exists in the Yersinia T3S system to accompany the FliM-sized cognate. The FliN-sized cognate, YscQ-C, is the product of an internal translation initiation site within the locus encoding the FliM-sized cognate YscQ. Both intact YscQ and YscQ-C were found to be required for T3S, indicating that the internal translation initiation site, which is conserved in some but not all YscQ orthologs, is crucial for function. The crystal structure of YscQ-C revealed a SpoA domain that forms a highly intertwined, domain-swapped homodimer, similar to those observed in FliN and the YscQ ortholog HrcQ(B). A single YscQ-C homodimer associated reversibly with a single molecule of intact YscQ, indicating conformational differences between the SpoA domains of intact YscQ and YscQ-C. A "snap-back" mechanism suggested by the structure can account for this. The 1:2 YscQ-YscQ-C complex is a close mimic of the 1:4 FliM-FliN complex and the likely building block of the putative Yersinia T3S system C-ring. PubMed: 22320351DOI: 10.1021/bi201792p 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.25 Å) |
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