Structural highlights
Function
Q9X4B7_ECOLX
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Distance fingerprinting: Pulsed electron-electron double resonance spectroscopy (PELDOR) is applied to the octameric membrane protein complex Wza of E. coli. The data yielded a detailed distance fingerprint of its periplasmic region that compares favorably to the crystal structure. These results provide the foundation to study conformation changes from interaction with partner proteins.
PELDOR Spectroscopy Distance Fingerprinting of the Octameric Outer-Membrane Protein Wza from Escherichia coli.,Hagelueken G, Ingledew WJ, Huang H, Petrovic-Stojanovska B, Whitfield C, Elmkami H, Schiemann O, Naismith JH Angew Chem Int Ed Engl. 2009 Mar 17;48(16):2904-2906. PMID:19294709[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hagelueken G, Ingledew WJ, Huang H, Petrovic-Stojanovska B, Whitfield C, Elmkami H, Schiemann O, Naismith JH. PELDOR Spectroscopy Distance Fingerprinting of the Octameric Outer-Membrane Protein Wza from Escherichia coli. Angew Chem Int Ed Engl. 2009 Mar 17;48(16):2904-2906. PMID:19294709 doi:10.1002/anie.200805758
