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