2LME

Solid-state NMR structure of the membrane anchor domain of the trimeric autotransporter YadA

Summary for 2LME

• Entry DOI: 10.2210/pdb2lme/pdb
• NMR Information: BMRB: 18108
• Descriptor: Adhesin yadA (1 entity in total)
• Functional Keywords: trimeric autotransporter, membrane protein, cell adhesion
• Biological source: Yersinia enterocolitica subsp. enterocolitica
• Cellular location: Cell outer membrane (By similarity): A1JUB7
• Total number of polymer chains: 3
• Total formula weight: 33865.40

Authors

Shahid, S.A.,Bardiaux, B.,Franks, W.T.,Habeck, M.,Linke, D.,van Rossum, B. (deposition date: 2011-11-30, release date: 2012-11-07, Last modification date: 2024-05-15)

Primary citation

Shahid, S.A.,Bardiaux, B.,Franks, W.T.,Krabben, L.,Habeck, M.,van Rossum, B.J.,Linke, D.
Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals.
Nat.Methods, 9:1212-1217, 2012

PubMed Abstract: 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.

PubMed: 23142870
DOI: 10.1038/nmeth.2248

Experimental method

SOLID-STATE NMR