2hhk

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Reaction centre from Rhodobacter sphaeroides strain R-26.1 complexed with dibrominated phosphatidylglycerol

Overview

This study describes the use of brominated phospholipids to distinguish, between lipid and detergent binding sites on the surface of a typical, alpha-helical membrane protein. Reaction centers isolated from Rhodobacter, sphaeroides were cocrystallized with added brominated phospholipids. X-ray, structural analysis of these crystals has revealed the presence of two, lipid binding sites from the characteristic strong X-ray scattering from, the bromine atoms. These results demonstrate the usefulness of this, approach to mapping lipid binding sites at the surface of membrane, proteins.

About this Structure

2HHK is a Protein complex structure of sequences from Rhodobacter sphaeroides with FE, K, CL, PO4, BCL, BPH, U10, CDL, PGT, PGK, LDA and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Brominated Lipids Identify Lipid Binding Sites on the Surface of the Reaction Center from Rhodobacter sphaeroides., Roszak AW, Gardiner AT, Isaacs NW, Cogdell RJ, Biochemistry. 2007 Mar 20;46(11):2909-16. Epub 2007 Feb 23. PMID:17315985

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