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Cited by 413

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex

Open access
Essen, L.-O., Siegert, R., Lehmann, W. D., Oesterhelt, D.·1998·Proceedings of the National Academy of Sciences

Abstract

Heterogenous nucleation on small molecule crystals causes a monoclinic crystal form of bacteriorhodopsin (BR) in which trimers of this membrane protein pack differently than in native purple membranes. Analysis of single crystals by nano-electrospray ionization-mass spectrometry demonstrated a preservation of the purple membrane lipid composition in these BR crystals. The 2.9-Å x-ray structure shows a lipid-mediated stabilization of BR trimers where the glycolipid S-TGA-1 binds into the central compartment of BR trimers. The BR trimer/lipid complex provides an example of local membrane thinning as the lipid head-group boundary of the central lipid patch is shifted by 5 Å toward the membrane center. Nonbiased electron density maps reveal structural differences to previously reported BR structures, especially for the cytosolic EF loop and the proton exit pathway. The terminal proton release complex now comprises an E194-E204 dyad as a diffuse proton buffer.

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Metadata

Authors
Essen, L.-O., Siegert, R., Lehmann, W. D., & Oesterhelt, D.
Venue
Proceedings of the National Academy of Sciences
Published
1998-09-29
Volume
95
Issue
20
Pages
11673-11678
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2019306938
Cited by
413
References
1
FWCI
15.14
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex. https://app.cochat.ai/papers/10.1073/pnas.95.20.11673
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Essen, L.-O., Siegert, R., Lehmann, W. D., & Oesterhelt, D. (1998). Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.20.11673

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