PMID- 1892841
OWN - NLM
STAT- MEDLINE
DCOM- 19911024
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 30
IP  - 39
DP  - 1991 Oct 1
TI  - Structure of the detergent phase and protein-detergent interactions in crystals 
      of the wild-type (strain Y) Rhodobacter sphaeroides photochemical reaction 
      center.
PG  - 9403-13
AB  - Rhodobacter sphaeroides (strain Y) reaction center (RC) crystals were grown in 
      the presence of n-octyl beta-glucoside (beta-OG). In order to determine the 
      structure of the detergent phase in these crystals, low-resolution neutron 
      diffraction experiments were performed at different contrasts obtained by varying 
      the H2O/D2O ratio in the solvent. From the contrast variation data and from the 
      RC atomic coordinates determined by X-ray diffraction [Arnoux, B., Ducruix, A., 
      Reiss-Husson, F., Lutz, M., Norris, J., Schiffer, M., & Chang, C. H. (1989) FEBS 
      Lett. 258, 47-50], a model was obtained for the structure of the detergent phase 
      in the crystal. The detergent forms a ring-shaped micelle surrounding the most 
      hydrophobic part of the transmembrane alpha helices of the RC. Each detergent 
      ring is connected to two next-neighbor rings by intermicellar bridges. The 
      detergent phase is organized thus in infinite zigzag chains parallel to the b 
      axis of the P2(1)2(1)2(1) unit cell. The main interactions between beta-OG 
      molecules and the RC molecules are hydrophobic and are localized at the level of 
      the transmembrane alpha helices. This interaction replaces the 
      phospholipid-protein interaction existing in vivo in the membrane and, to some 
      extent, also the light harvesting complex-protein interaction. Secondary 
      hydrophilic interactions are found between a few of the charged residues of the H 
      subunit and the hydrophilic surface of the detergent ring from a neighboring RC 
      molecule. A comparison with a previous study on Rhodopseudomonas viridis crystals 
      [which grow in the presence of lauryldimethylamine N-oxide (LDAO) and belong to a 
      different space group] [Roth, M., Lewit-Bentley, A., Michel, H., Deisenhofer, J., 
      Huber, R., & Oesterhelt, D. (1989) Nature 340, 659-661] shows a quasi identity of 
      shape and position of the beta-OG and LDAO rings around the transmembrane alpha 
      helices. The secondary interactions, involving in both cases the external surface 
      of the H subunit, differ because of the different molecular packing in the two 
      space groups. The role and structural requirements of the detergent in the 
      crystallization process are discussed.
FAU - Roth, M
AU  - Roth M
AD  - Laboratoire d'Ingenierie des Proteines, LIP/LCCP, Centre d'Etudes Nucleaires de 
      Grenoble, France.
FAU - Arnoux, B
AU  - Arnoux B
FAU - Ducruix, A
AU  - Ducruix A
FAU - Reiss-Husson, F
AU  - Reiss-Husson F
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Detergents)
RN  - 0 (Glucosides)
RN  - 0 (Photosynthetic Reaction Center Complex Proteins)
RN  - 29836-26-8 (octyl-beta-D-glucoside)
SB  - IM
MH  - Algorithms
MH  - Computer Graphics
MH  - Crystallography
MH  - Detergents/*chemistry
MH  - Glucosides/*chemistry
MH  - Models, Molecular
MH  - Neutrons
MH  - Photosynthetic Reaction Center Complex Proteins/*chemistry
MH  - Rhodobacter sphaeroides/*analysis
MH  - Scattering, Radiation
MH  - Species Specificity
EDAT- 1991/10/01 00:00
MHDA- 1991/10/01 00:01
CRDT- 1991/10/01 00:00
PHST- 1991/10/01 00:00 [pubmed]
PHST- 1991/10/01 00:01 [medline]
PHST- 1991/10/01 00:00 [entrez]
AID - 10.1021/bi00103a003 [doi]
PST - ppublish
SO  - Biochemistry. 1991 Oct 1;30(39):9403-13. doi: 10.1021/bi00103a003.