1m8m: Difference between revisions

Revision as of 14:52, 21 February 2008

SOLID-STATE MAS NMR STRUCTURE OF THE A-SPECTRIN SH3 DOMAIN

OverviewOverview

The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not accessible to solution NMR, such as amyloid systems or membrane proteins. Here we present a protein structure determined by solid-state magic-angle-spinning (MAS) NMR. Almost complete (13)C and (15)N resonance assignments for a micro-crystalline preparation of the alpha-spectrin Src-homology 3 (SH3) domain formed the basis for the extraction of a set of distance restraints. These restraints were derived from proton-driven spin diffusion (PDSD) spectra of biosynthetically site-directed, labelled samples obtained from bacteria grown using [1,3-(13)C]glycerol or [2-(13)C]glycerol as carbon sources. This allowed the observation of long-range distance correlations up to approximately 7 A. The calculated global fold of the alpha-spectrin SH3 domain is based on 286 inter-residue (13)C-(13)C and six (15)N-(15)N restraints, all self-consistently obtained by solid-state MAS NMR. This MAS NMR procedure should be widely applicable to small membrane proteins that can be expressed in bacteria.

About this StructureAbout this Structure

1M8M is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy., Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H, Nature. 2002 Nov 7;420(6911):98-102. PMID:12422222

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-[[Image:1m8m.jpg|left|200px]]<br /><applet load="1m8m" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1m8m" />
 '''SOLID-STATE MAS NMR STRUCTURE OF THE A-SPECTRIN SH3 DOMAIN'''<br />
 ==Overview==
-The determination of a representative set of protein structures is a chief, aim in structural genomics. Solid-state NMR may have a crucial role in, structural investigations of those proteins that do not easily form, crystals or are not accessible to solution NMR, such as amyloid systems or, membrane proteins. Here we present a protein structure determined by, solid-state magic-angle-spinning (MAS) NMR. Almost complete (13)C and, (15)N resonance assignments for a micro-crystalline preparation of the, alpha-spectrin Src-homology 3 (SH3) domain formed the basis for the, extraction of a set of distance restraints. These restraints were derived, from proton-driven spin diffusion (PDSD) spectra of biosynthetically, site-directed, labelled samples obtained from bacteria grown using, [1,3-(13)C]glycerol or [2-(13)C]glycerol as carbon sources. This allowed, the observation of long-range distance correlations up to approximately 7, A. The calculated global fold of the alpha-spectrin SH3 domain is based on, 286 inter-residue (13)C-(13)C and six (15)N-(15)N restraints, all, self-consistently obtained by solid-state MAS NMR. This MAS NMR procedure, should be widely applicable to small membrane proteins that can be, expressed in bacteria.
+The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not accessible to solution NMR, such as amyloid systems or membrane proteins. Here we present a protein structure determined by solid-state magic-angle-spinning (MAS) NMR. Almost complete (13)C and (15)N resonance assignments for a micro-crystalline preparation of the alpha-spectrin Src-homology 3 (SH3) domain formed the basis for the extraction of a set of distance restraints. These restraints were derived from proton-driven spin diffusion (PDSD) spectra of biosynthetically site-directed, labelled samples obtained from bacteria grown using [1,3-(13)C]glycerol or [2-(13)C]glycerol as carbon sources. This allowed the observation of long-range distance correlations up to approximately 7 A. The calculated global fold of the alpha-spectrin SH3 domain is based on 286 inter-residue (13)C-(13)C and six (15)N-(15)N restraints, all self-consistently obtained by solid-state MAS NMR. This MAS NMR procedure should be widely applicable to small membrane proteins that can be expressed in bacteria.
 ==About this Structure==
-M8M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M8M OCA].
+M8M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8M OCA].
 ==Reference==
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 [[Category: Oschkinat, H.]]
 [[Category: Rehbein, K.]]
-[[Category: Rossum, B.Van.]]
+[[Category: Rossum, B Van.]]
 [[Category: Schubert, M.]]
 [[Category: solid-state mas nmr structure]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:13:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:44 2008''