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Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals.
MedLine Citation:
PMID:  23142870     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Shakeel Ahmad Shahid; Benjamin Bardiaux; W Trent Franks; Ludwig Krabben; Michael Habeck; Barth-Jan van Rossum; Dirk Linke
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-11
Journal Detail:
Title:  Nature methods     Volume:  -     ISSN:  1548-7105     ISO Abbreviation:  Nat. Methods     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101215604     Medline TA:  Nat Methods     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
1] Leibniz-Institut für Molekulare Pharmakologie, Abteilung Strukturbiologie, Berlin, Germany. [2] Max-Planck-Institut für Entwicklungsbiologie, Abteilung Proteinevolution, Tübingen, Germany. [3].
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