2lgi: Difference between revisions
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==Atomic Resolution Protein Structures using NMR Chemical Shift Tensors== | ==Atomic Resolution Protein Structures using NMR Chemical Shift Tensors== | ||
<StructureSection load='2lgi' size='340' side='right'caption='[[2lgi | <StructureSection load='2lgi' size='340' side='right'caption='[[2lgi]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2lgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LGI FirstGlance]. <br> | ||
</td></tr> | </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=2lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgi OCA], [https://pdbe.org/2lgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lgi RCSB], [https://www.ebi.ac.uk/pdbsum/2lgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgi ProSAT]</span></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=2lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgi OCA], [https://pdbe.org/2lgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lgi RCSB], [https://www.ebi.ac.uk/pdbsum/2lgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgi ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus sp. 'group G']] | ||
[[Category: Franks | [[Category: Franks WT]] | ||
[[Category: Nieuwkoop | [[Category: Nieuwkoop AJ]] | ||
[[Category: Oldfield | [[Category: Oldfield E]] | ||
[[Category: Rienstra | [[Category: Rienstra CM]] | ||
[[Category: Sperling | [[Category: Sperling LJ]] | ||
[[Category: Wylie | [[Category: Wylie BJ]] | ||
Revision as of 13:58, 15 February 2023
Atomic Resolution Protein Structures using NMR Chemical Shift TensorsAtomic Resolution Protein Structures using NMR Chemical Shift Tensors
Structural highlights
FunctionSPG1_STRSG Binds to the constant Fc region of IgG with high affinity. Publication Abstract from PubMedNMR chemical shift tensors (CSTs) in proteins, as well as their orientations, represent an important new restraint class for protein structure refinement and determination. Here, we present the first determination of both CST magnitudes and orientations for (13)Calpha and (15)N (peptide backbone) groups in a protein, the beta1 IgG binding domain of protein G from Streptococcus spp., GB1. Site-specific (13)Calpha and (15)N CSTs were measured using synchronously evolved recoupling experiments in which (13)C and (15)N tensors were projected onto the (1)H-(13)C and (1)H-(15)N vectors, respectively, and onto the (15)N-(13)C vector in the case of (13)Calpha. The orientations of the (13)Calpha CSTs to the (1)H-(13)C and (13)C-(15)N vectors agreed well with the results of ab initio calculations, with an rmsd of approximately 8 degrees . In addition, the measured (15)N tensors exhibited larger reduced anisotropies in alpha-helical versus beta-sheet regions, with very limited variation (18 +/- 4 degrees ) in the orientation of the z-axis of the (15)N CST with respect to the (1)H-(15)N vector. Incorporation of the (13)Calpha CST restraints into structure calculations, in combination with isotropic chemical shifts, transferred echo double resonance (13)C-(15)N distances and vector angle restraints, improved the backbone rmsd to 0.16 A (PDB ID code 2LGI) and is consistent with existing X-ray structures (0.51 A agreement with PDB ID code 2QMT). These results demonstrate that chemical shift tensors have considerable utility in protein structure refinement, with the best structures comparable to 1.0-A crystal structures, based upon empirical metrics such as Ramachandran geometries and chi(1)/chi(2) distributions, providing solid-state NMR with a powerful tool for de novo structure determination. Ultrahigh resolution protein structures using NMR chemical shift tensors.,Wylie BJ, Sperling LJ, Nieuwkoop AJ, Franks WT, Oldfield E, Rienstra CM Proc Natl Acad Sci U S A. 2011 Oct 11;108(41):16974-9. Epub 2011 Oct 3. PMID:21969532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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