1QOV

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M260 REPLACED WITH TRP (CHAIN M, A260W)

Summary for 1QOV

• Entry DOI: 10.2210/pdb1qov/pdb
• Related: 1AIG 1AIJ 1MPS 1PCR 1PSS 1PST 1YST 2RCR 4RCR
• Descriptor: PHOTOSYNTHETIC REACTION CENTER, CHLORIDE ION, BACTERIOCHLOROPHYLL A, ... (11 entities in total)
• Functional Keywords: photosynthetic reaction center, transmembrane, electron transport, photosynthesis, cardiolipin, membrane protein
• Biological source: RHODOBACTER SPHAEROIDES; More
• Total number of polymer chains: 3
• Total formula weight: 102364.51

Authors

McAuley, K.E.,Fyfe, P.K.,Ridge, J.P.,Isaacs, N.W.,Cogdell, R.J.,Jones, M.R. (deposition date: 1999-11-17, release date: 1999-12-13, Last modification date: 2024-05-01)

Primary citation

Mcauley, K.E.,Fyfe, P.K.,Ridge, J.P.,Isaacs, N.W.,Cogdell, R.J.,Jones, M.R.
Structural Details of an Interaction between Cardiolipin and an Integral Membrane Protein
Proc.Natl.Acad.Sci.USA, 96:14706-, 1999

PubMed Abstract: Anionic lipids play a variety of key roles in biomembrane function, including providing the immediate environment for the integral membrane proteins that catalyze photosynthetic and respiratory energy transduction. Little is known about the molecular basis of these lipid-protein interactions. In this study, x-ray crystallography has been used to examine the structural details of an interaction between cardiolipin and the photoreaction center, a key light-driven electron transfer protein complex found in the cytoplasmic membrane of photosynthetic bacteria. X-ray diffraction data collected over the resolution range 30.0-2.1 A show that binding of the lipid to the protein involves a combination of ionic interactions between the protein and the lipid headgroup and van der Waals interactions between the lipid tails and the electroneutral intramembrane surface of the protein. In the headgroup region, ionic interactions involve polar groups of a number of residues, the protein backbone, and bound water molecules. The lipid tails sit along largely hydrophobic grooves in the irregular surface of the protein. In addition to providing new information on the immediate lipid environment of a key integral membrane protein, this study provides the first, to our knowledge, high-resolution x-ray crystal structure for cardiolipin. The possible significance of this interaction between an integral membrane protein and cardiolipin is considered.

PubMed: 10611277
DOI: 10.1073/PNAS.96.26.14706

Experimental method

X-RAY DIFFRACTION (2.1 Å)