TAILIEUCHUNG - Báo cáo khoa học: Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen⁄deuterium exchange measurements

The translocation domain (T domain) of diphtheria toxin adopts a partially folded state, the so-called molten globule state, to become functional at acidic pH. We compared, using hydrogen⁄deuterium exchange experiments associated with MS, the structures of the T domain in its soluble folded state at neutral pH and in its functional molten globule state at acidic pH. | ỊFEBS Journal Accessibility changes within diphtheria toxin T domain when in the functional molten globule state as determined using hydrogen deuterium exchange measurements Petr Man1 2 z Caroline Montagner3 z Heidi Vitrac3 Daniel Kavan2 Sylvain Pichard4 Daniel Gillet4 Eric Forest1 and Vincent Forge3 1 Laboratoire de Spectrometrie de Masse des Proteines Institut de Biologie Structurale CEA CNRS UJF UMR 5075 Grenoble France 2 Laboratory of Molecular Structure Characterization Institute of Microbiology Academy of Sciences of the Czech Republic Videnska 1083 Prague 4 Czech Republic 3 CEA DSV iRTSV Laboratoire de Chimie et Biologie des Metaux UMR 5249 CEA-Grenoble Grenoble France 4 Commissariat à l Energie Atomique CEA Institut de Biologie et Technologies de Saclay iBiTecS Service d lngenierie Moleculaire des Proteines SIMOPRO F-91191 Gif sur Yvette France Keywords diphtheria toxin hydrogen deuterium exchanges mass spectrometry protein membrane interactions translocation domain Correspondence D. Gillet Commissariat a l Energie Atomique CEA Institut de Biologie et Technologies de Saclay iBiTecS Service d Ingenierie Moleculaire des Proteines SIMOPRO F-91191 Gif sur Yvette France Fax 33 1 69 08 94 30 Tel 33 1 69 08 76 46 E-mail E. Forest Laboratoire de Spectrometrie de Masse des Proteines Institut de Biologie Structurale CEA-CNRS-UJF 41 rue Jules Horowitz 38027 Grenoble France Fax 33 4 38 78 54 94 Tel 33 4 38 78 34 03 E-mail V. Forge CEA DSV iRTSV Laboratoire de Chimie et Biologie des Metaux UMR 5249 CEA-Grenoble 17 rue des martyrs 38054 Grenoble France Fax 33 4 38 78 54 87 Tel 33 4 38 78 94 05 E-mail The translocation domain T domain of diphtheria toxin adopts a partially folded state the so-called molten globule state to become functional at acidic pH. We compared using hydrogen deuterium exchange experiments associated with MS the structures of the T domain in its soluble folded state at neutral pH and in its

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