Crystal Structure of Osmoporin OmpC from E. coli at 2.0 Å

Porins form transmembrane pores in the outer membrane of Gram-negative bacteria with matrix porin OmpF and osmoporin OmpC from Escherichia coli being differentially expressed depending on environmental conditions. The three-dimensional structure of OmpC has been determined to 2.0 Å resolution by X-r...

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Veröffentlicht in:	Journal of molecular biology 2006-10, Vol.362 (5), p.933-942
Hauptverfasser:	Baslé, Arnaud, Rummel, Gabriele, Storici, Paola, Rosenbusch, Juerg P., Schirmer, Tilman
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - isolation & purification Binding Sites crystal structure Crystallography, X-Ray Escherichia coli Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - isolation & purification Hydrogen Bonding Models, Chemical Molecular Sequence Data OmpC osmoporin outer membrane porin Porins - chemistry Protein Binding Protein Conformation Protein Folding Protein Structure, Secondary Sequence Homology, Amino Acid Water - chemistry
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