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TitleStudying Conformational Changes of the Yersinia Type-III-Secretion Effector YopO in Solution by Integrative Structural Biology.
Journal, issue, pagesStructure, Vol. 27, Issue 9, Page 1416-11426.e3, Year 2019
Publish dateSep 3, 2019
AuthorsMartin F Peter / Anne T Tuukkanen / Caspar A Heubach / Alexander Selsam / Fraser G Duthie / Dmitri I Svergun / Olav Schiemann / Gregor Hagelueken /
PubMed AbstractThe type-III secretion effector YopO helps pathogenic Yersinia to outmaneuver the human immune system. Injected into host cells, it functions as a Ser/Thr kinase after activation by actin binding. ...The type-III secretion effector YopO helps pathogenic Yersinia to outmaneuver the human immune system. Injected into host cells, it functions as a Ser/Thr kinase after activation by actin binding. This activation process is thought to involve large conformational changes. We use PELDOR spectroscopy and small-angle X-ray scattering in combination with available crystal structures to study these conformational transitions. Low-resolution hybrid models of the YopO/actin structure in solution were constructed, where the kinase domain of YopO is tilted "backward" compared with the crystal structure, thus shortening the distance between actin and the kinase active site, potentially affecting the substrate specificity of YopO. Furthermore, the GDI domain of the hybrid models resembles a conformation that was previously observed in a crystal structure of the isolated GDI domain. We investigate possible structural reasons for the inactivity of the apo state, analyze its flexibility and discuss the biological implications.
External linksStructure / PubMed:31303480
MethodsSAS (X-ray synchrotron)
Structure data

SASDFC6:
Wild type protein kinase YopO (Protein kinase YopO, YopO)
Method: SAXS/SANS

SASDFD6:
Protein kinase YopO - cytoplasmic 1 actin complex (Protein kinase YopO, YopO + Actin, cytoplasmic 1, Actin)
Method: SAXS/SANS

Source
  • Yersinia enterocolitica (bacteria)
  • Homo sapiens (human)

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