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[[Image:2gi9.gif|left|200px]]<br /><applet load="2gi9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2gi9, resolution 1.14&Aring;" />
'''Backbone Conformational Constraints in a Microcrystalline U-15N-Labeled Protein by 3D Dipolar-Shift Solid-State NMR Spectroscopy'''<br />


==Overview==
==Backbone Conformational Constraints in a Microcrystalline U-15N-Labeled Protein by 3D Dipolar-Shift Solid-State NMR Spectroscopy==
Structural studies of uniformly labeled proteins by magic-angle spinning NMR spectroscopy have rapidly matured in recent years. Site-specific chemical shifts of several proteins have been assigned and structures determined from 2D or 3D data sets containing internuclear distance information. Here we demonstrate the application of a complementary technique for constraining protein backbone geometry using a site-resolved 3D dipolar-shift pulse sequence. The dipolar line shapes report on the relative orientations of 1H-15N[i] to 1H-15N[i+1] dipole vectors, constraining the torsion angles phi[i] and psi[i]. In addition, from the same 3D data set, several 1H-15N[i] to1H-15N[i+2] line shapes are extracted to constrain the torsion angles phi[i], psi[i], phi[i+1], and psi[i+1]. We report results for the majority of sites in the 56-residue beta1 immunoglobulin binding domain of protein G (GB1), using 3D experiments at 600 MHz 1H frequency. Excellent agreement between the SSNMR results and a new 1.14 A crystal structure illustrate the general potential of this technique for high-resolution structural refinement of solid proteins.
<StructureSection load='2gi9' size='340' side='right'caption='[[2gi9]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gi9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GI9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gi9 OCA], [https://pdbe.org/2gi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gi9 RCSB], [https://www.ebi.ac.uk/pdbsum/2gi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gi9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG]  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gi/2gi9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gi9 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2GI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GI9 OCA].
*[[Protein G|Protein G]]
 
__TOC__
==Reference==
</StructureSection>
Backbone conformational constraints in a microcrystalline U-15N-labeled protein by 3D dipolar-shift solid-state NMR spectroscopy., Franks WT, Wylie BJ, Stellfox SA, Rienstra CM, J Am Chem Soc. 2006 Mar 15;128(10):3154-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16522090 16522090]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Franks, W T.]]
[[Category: Franks WT]]
[[Category: Rienstra, C M.]]
[[Category: Rienstra CM]]
[[Category: Stellfox, S A.]]
[[Category: Stellfox SA]]
[[Category: Wylie, B J.]]
[[Category: Wylie BJ]]
[[Category: gb1]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:56 2008''

Latest revision as of 09:28, 14 February 2024

Backbone Conformational Constraints in a Microcrystalline U-15N-Labeled Protein by 3D Dipolar-Shift Solid-State NMR Spectroscopy

2gi9, resolution 1.14Å

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