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РЖ ВИНИТИ 34 (BI12) 95.11-04Б2.43

Rotational orientation of transmembrane 'альфа'-helices in bacteriorhodopsin. A neutron diffraction study [Text] / Fadel A. Samatey [et al.] // J. Mol. Biol. - 1994. - Vol. 236, N 4. - P1093-1104 . - ISSN 0022-2836
Перевод заглавия: Вращательная ориентация трансмембранных 'альфа'-спиралей в бактериородопсине. Изучение с помощью дифракции нейтронов
Аннотация: The rotational orientation of the seven transmembrane 'альфа'-helices (A-G) in bacteriorhodopsin has been investigated by neutron diffraction. The current model of bacteriorhodopsin is based on an electron density map obtained by high-resolution electron microscopy (EM). Assigning helix rotational positions in the EM model depended on fitting large side-chains, mainly aromatic residues, into bulges in the electron density map. For helix D, which contains no aromatic residues, the EM map is more difficult to interpret. For helices A and B, whose position and orientation had been determined previously by neutron diffraction, the positions defined by AM agree within experimental error with these earlier conclusions. The orientation of all seven helices has been examined by using meutron diffraction on bacteriorhodopsin samples with specifically deuterated valine, leucine and tryptophan residues. Experimental peak intensities were compared to those predicted for an extensive set of structural models. The models were generated by (1) rotating all helices around their axis; (2) moving deuterated residues in the extramembrane loops about their probable positions and changing the weight of their contribution to the neutron diffraction pattern; (3) allowing deuterated side-chains to change their conformation. The analysis confirmed exactly the positions previously determined for helices A and B. For an optimal fit to the data to be obrained, the other five helices, including helix D, must lie either at or within 20'ГРАДУС' of their position in the current EM model. The complementarity of medium-resolution EM, neutron diffraction and model building for the structural study of integral membrane proteins is discussed. Франция, Inst. Laue-Langevin, BP 156X, avenue des Martyrs F-38042 Grenoble. Библ. 41

ГРНТИ	34.27.17

ВИНИТИ 341.27.17.09.07.09.29
Рубрики: БАКТЕРИОРОДОПСИНЫ
ТРАНСМЕМБРАННЫЕ АЛЬФА-СПИРАЛИ
МЕТОД ДИФРАКЦИИ НЕЙТРОНОВ

Доп.точки доступа:
Samatey, Fadel A.; Zaccai, Giuseppe; Engelman, Donald M.; Etchebest, Catherine; Popot, Jean-Luc

РЖ ВИНИТИ 34 (BI12) 95.12-04Б2.73

Rotational orientation of transmembrane 'альфа'-helices in bacteriorhodopsin. A neutron diffraction study [Text] / Fadel A. Samatey [et al.] // J. Mol. Biol. - 1994. - Vol. 236, N 4. - P1093-1104 . - ISSN 0022-2836
Перевод заглавия: Вращательная ориентация трансмембранных 'альфа'-спиралей в бактериородопсине. Изучение с помощью дифракции нейтронов
Аннотация: The rotational orientation of the seven transmembrane 'альфа'-helices (A-G) in bacteriorhodopsin has been investigated by neutron diffraction. The current model of bacteriorhodopsin is based on an electron density map obtained by high-resolution electron microscopy (EM). Assigning helix rotational positions in the EM model depended on fitting large side-chains, mainly aromatic residues, into bulges in the electron density map. For helix D, which contains no aromatic residues, the EM map is more difficult to interpret. For helices A and B, whose position and orientation had been determined previously by neutron diffraction, the positions defined by AM agree within experimental error with these earlier conclusions. The orientation of all seven helices has been examined by using meutron diffraction on bacteriorhodopsin samples with specifically deuterated valine, leucine and tryptophan residues. Experimental peak intensities were compared to those predicted for an extensive set of structural models. The models were generated by (1) rotating all helices around their axis; (2) moving deuterated residues in the extramembrane loops about their probable positions and changing the weight of their contribution to the neutron diffraction pattern; (3) allowing deuterated side-chains to change their conformation. The analysis confirmed exactly the positions previously determined for helices A and B. For an optimal fit to the data to be obrained, the other five helices, including helix D, must lie either at or within 20'ГРАДУС' of their position in the current EM model. The complementarity of medium-resolution EM, neutron diffraction and model building for the structural study of integral membrane proteins is discussed. Франция, Inst. Laue-Langevin, BP 156X, avenue des Martyrs F-38042 Grenoble. Библ. 41

ГРНТИ	34.27.17

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