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-Structure paper
タイトル | Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD. |
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ジャーナル・号・ページ | J Biol Chem, Vol. 282, Issue 6, Page 4035-4044, Year 2007 |
掲載日 | 2007年2月9日 |
![]() | Steven Johnson / Pietro Roversi / Marianela Espina / Andrew Olive / Janet E Deane / Susan Birket / Terry Field / William D Picking / Ariel J Blocker / Edouard E Galyov / Wendy L Picking / Susan M Lea / ![]() |
PubMed 要旨 | Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. ...Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence: IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intramolecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure. |
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手法 | X線回折 |
解像度 | 2.1 - 3.1 Å |
構造データ | ![]() PDB-2ixr: ![]() PDB-2j0n: ![]() PDB-2j0o: ![]() PDB-2j9t: ![]() PDB-2jaa: |
化合物 | ![]() ChemComp-HOH: ![]() ChemComp-GOL: ![]() ChemComp-BO3: ![]() ChemComp-FLC: |
由来 |
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![]() | TOXIN / BURKHOLDERIA PSEUDOMALLEI / BIPD / TTSS / T3SS / TYPE 3 SECRETION SYSTEM / CELL INVASION / IPAD / PLASMID / VIRULENCE / SHIGELLA FLEXNERI / TYPE III SECRETION / INVASIN / SEMET |