Effect of the C‐terminal proline repeats on ordered packing of squid rhodopsin and its mobility in membranes

FEBS Letters

Venien-Bryan, Catherine⁴  Saibil, Helen³  Davies, Anthony³  Watts, Anthony⁴  Langmack, Keith²  Marsh, Derek¹  Baverstock, Jenny² 

[1] Abt. Spektroskopie, Max Planck Institut für Biophysikalische Chemie, D-37077 Göttingen, Germany;Zoology Department, Oxford University, Oxford, OX1 3PS, UK;Crystallography Department, Birkbeck College London, London, WC1E 7HX, UK;Biochemistry Department, Oxford University, Oxford, OX1 3QU, UK

关键词: 2D crystal;    Negative stain electron microscopy;    Spin label ESR (spectroscopy);    Rotational diffusion;    Cephalopod rhodopsin;   

DOI  :  10.1016/0014-5793(94)01449-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Negative stain electron microscopy and saturation transfer electron spin resonance spectroscopy have been used to compare the lattice ordering and in-plane membrane mobility of full-length and C-terminally cleaved squid rhodopsin. The C-terminus of squid rhodopsin contains a negatively charged region followed by 9–10 repeats of a proline-rich sequence, not found in rhodopsins other than those of cephalopod invertebrates, but similar proline repeats are found in other, unrelated membrane proteins. We find that the proline repeats cluster the rhodopsins into small groups, interfering with two-dimensional crystallization and maintaining their mobility in the membrane.

【 授权许可】

Unknown