5ITE
2.2-Angstrom in meso crystal structure of Haloquadratum Walsbyi Bacteriorhodopsin (HwBR) from Octylglucoside (OG) Detergent Micelles
Summary for 5ITE
| Entry DOI | 10.2210/pdb5ite/pdb |
| Related | 5ITC |
| Descriptor | Bacteriorhodopsin-I, RETINAL, (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total) |
| Functional Keywords | bacteriorhodopsin from haloquadratum walsbyi, lipidic cubic phase (lcp), og detergent micelle, traditional, membrane protein |
| Biological source | Haloquadratum walsbyi |
| Cellular location | Cell membrane ; Multi-pass membrane protein : Q18DH8 |
| Total number of polymer chains | 3 |
| Total formula weight | 91364.60 |
| Authors | Broecker, J.,Eger, B.T.,Ernst, O.P. (deposition date: 2016-03-16, release date: 2017-01-25, Last modification date: 2024-11-06) |
| Primary citation | Broecker, J.,Eger, B.T.,Ernst, O.P. Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs. Structure, 25:384-392, 2017 Cited by PubMed Abstract: For some membrane proteins, detergent-mediated solubilization compromises protein stability and functionality, often impairing biophysical and structural analyses. Hence, membrane-protein structure determination is a continuing bottleneck in the field of protein crystallography. Here, as an alternative to approaches mediated by conventional detergents, we report the crystallogenesis of a recombinantly produced membrane protein that never left a lipid bilayer environment. We used styrene-maleic acid (SMA) copolymers to solubilize lipid-embedded proteins into SMA nanodiscs, purified these discs by affinity and size-exclusion chromatography, and transferred proteins into the lipidic cubic phase (LCP) for in meso crystallization. The 2.0-Å structure of an α-helical seven-transmembrane microbial rhodopsin thus obtained is of high quality and virtually identical to the 2.2-Å structure obtained from traditional detergent-based purification and subsequent LCP crystallization. PubMed: 28089451DOI: 10.1016/j.str.2016.12.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.182 Å) |
Structure validation
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