3POQ: Crystal Structure Of E.Coli Ompf Porin In Lipidic Cubic Phase: Space Group H32, Small Unit Cell

Citation:
Abstract
Outer membrane protein F, a major component of the Escherichia coli outer membrane, was crystallized for the first time in lipidic mesophase of monoolein in novel space groups, P1 and H32. Due to ease of its purification and crystallization OmpF can be used as a benchmark protein for establishing membrane protein crystallization in meso, as a "membrane lyzozyme". The packing of porin trimers in the crystals of space group H32 is similar to natural outer membranes, providing the first high-resolution insight into the close to native packing of OmpF. Surprisingly, interaction between trimers is mediated exclusively by lipids, without direct protein-protein contacts. Multiple ordered lipids are observed and many of them occupy identical positions independently of the space group, identifying preferential interaction sites of lipid acyl chains. Presence of ordered aliphatic chains close to a positively charged area on the porin surface suggests a position for a lipopolysaccharide binding site on the surface of the major E. coli porins.
PDB ID: 3POQDownload
MMDB ID: 97740
PDB Deposition Date: 2010/11/23
Updated in MMDB: 2012/06
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3POQ: trimeric; determined by author and by software (PISA)
Molecular Components in 3POQ
Label Count Molecule
Proteins (3 molecules)
3
Ompf Protein
Molecule annotation
Chemicals (66 molecules)
1
57
2
9
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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