Structural highlights
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Function
[YADA_YERE8] Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance (By similarity).
Publication Abstract from PubMed
Membrane proteins are largely underrepresented among available atomic-resolution structures. The use of detergents in protein purification procedures hinders the formation of well-ordered crystals for X-ray crystallography and leads to slower molecular tumbling, impeding the application of solution-state NMR. Solid-state magic-angle spinning NMR spectroscopy is an emerging method for membrane-protein structural biology that can overcome these technical problems. Here we present the solid-state NMR structure of the transmembrane domain of the Yersinia enterocolitica adhesin A (YadA). The sample was derived from crystallization trials that yielded only poorly diffracting microcrystals. We solved the structure using a single, uniformly (13)C- and (15)N-labeled sample. In addition, solid-state NMR allowed us to acquire information on the flexibility and mobility of parts of the structure, which, in combination with evolutionary conservation information, presents new insights into the autotransport mechanism of YadA.
Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals.,Shahid SA, Bardiaux B, Franks WT, Krabben L, Habeck M, van Rossum BJ, Linke D Nat Methods. 2012 Dec 7;9(12):1212-7. doi: 10.1038/nmeth.2248. Epub 2012 Nov 11. PMID:23142870[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shahid SA, Bardiaux B, Franks WT, Krabben L, Habeck M, van Rossum BJ, Linke D. Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals. Nat Methods. 2012 Dec 7;9(12):1212-7. doi: 10.1038/nmeth.2248. Epub 2012 Nov 11. PMID:23142870 doi:http://dx.doi.org/10.1038/nmeth.2248
