Can the low-resolution structures of photointermediates of bacteriorhodopsin explain their crystal structures?

ABSTRACT: To understand the molecular mechanism of light-driven proton pumps, the structures of the photointermediates of bacteriorhodopsin have been intensively investigated. Low-resolution diffraction techniques have demonstrated substantial conformational changes at the helix level in the M and N intermediates, between which there are noticeable differences. The intermediate structures at atomic resolution have also been solved by x-ray crystallography. Although the crystal structures have demonstrated local structural changes, such as hydrogen bond network rearrangements including water molecules, the large conformational changes at the helix level are not necessarily observed. Furthermore, the two reported crystal structures of an intermediate accumulated using a common method were distinct. To

SUBMITTER: Kamikubo H 

PROVIDER: S-EPMC1305245 | biostudies-literature | 2005 Mar

REPOSITORIES: biostudies-literature