Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements

0340829 - MBÚ 2010 RIV GB eng J - Článek v odborném periodiku
Man, Petr - Montagner, C. - Vitrac, H. - Kavan, Daniel - Pichard, S. - Gillet, D. - Forest, E. - Forge, V.
Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements.
FEBS Journal. Roč. 277, č. 3 (2010), s. 653-662. ISSN 1742-464X. E-ISSN 1742-4658
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: diphtheria toxin * hydrogen/deuterium exchanges * mass spectrometry
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.129, rok: 2010

ydrogen/Deuterium exchange coupled to mass spectrometry was used to describe pH driven unfolding of translocation domain from diphtheria toxin. Deuteration kinetics of two states, native-like at pH 7, and molten globule, at pH 4, were followed. In the native like state, helices TH5 and 8 were identified as the core of the protein. Surprisingly, this core is partially preserved even in the molten globule state which is usually characterized by the loss of tertiary structure. In addition, deuteration kinetics at pH 4 discovered surprising behavior of the interconnecting loop TL8-9. This part, which is supposed to be responsible for the insertion of the toxin into the lipid membrane forms oligomerization surface when the membrane is absent. These findings provide new insight into self-assembly of bacterial toxins
Trvalý link: http://hdl.handle.net/11104/0183992