9b4w: Difference between revisions
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==4F-Trp labeled Oscillatoria Agardhii Agglutinin (OAA)== | |||
<StructureSection load='9b4w' size='340' side='right'caption='[[9b4w]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9b4w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Planktothrix_agardhii Planktothrix agardhii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9B4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9B4W FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR, 10 models</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4FW:4-FLUOROTRYPTOPHANE'>4FW</scene></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=9b4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9b4w OCA], [https://pdbe.org/9b4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9b4w RCSB], [https://www.ebi.ac.uk/pdbsum/9b4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9b4w ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C0STD7_PLAAG C0STD7_PLAAG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Traditional protein structure determination by magic angle spinning (MAS) solid-state NMR spectroscopy primarily relies on interatomic distances up to 8 A, extracted from (13)C-, (15)N-, and (1)H-based dipolar-based correlation experiments. Here, we show that (19)F fast (60 kHz) MAS NMR spectroscopy can supply additional, longer distances. Using 4F-Trp,U-(13)C,(15)N crystalline Oscillatoria agardhii agglutinin (OAA), we demonstrate that judiciously designed 2D and 3D (19)F-based dipolar correlation experiments such as (H)CF, (H)CHF, and FF can yield interatomic distances in the 8-16 A range. Incorporation of fluorine-based restraints into structure calculation improved the precision of Trp side chain conformations as well as regions in the protein around the fluorine containing residues, with notable improvements observed for residues in proximity to the Trp pairs (W10/W17 and W77/W84) in the carbohydrate-binding loops, which lacked sufficient long-range (13)C-(13)C distance restraints. Our work highlights the use of fluorine and (19)F fast MAS NMR spectroscopy as a powerful structural biology tool. | |||
Integrating (19)F Distance Restraints for Accurate Protein Structure Determination by Magic Angle Spinning NMR Spectroscopy.,Runge BR, Zadorozhnyi R, Quinn CM, Russell RW, Lu M, Antolinez S, Struppe J, Schwieters CD, Byeon IL, Hadden-Perilla JA, Gronenborn AM, Polenova T J Am Chem Soc. 2024 Oct 23. doi: 10.1021/jacs.4c11373. PMID:39440810<ref>PMID:39440810</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9b4w" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Planktothrix agardhii]] | |||
[[Category: Antolinez S]] | |||
[[Category: Byeon IL]] | |||
[[Category: Gronenborn AM]] | |||
[[Category: Hadden-Perilla J]] | |||
[[Category: Lu M]] | |||
[[Category: Polenova T]] | |||
[[Category: Quinn CM]] | |||
[[Category: Runge BR]] | |||
[[Category: Russell RW]] | |||
[[Category: Schwieters CD]] | |||
[[Category: Struppe J]] | |||
[[Category: Zadorozhnyi RR]] | |||
Latest revision as of 11:13, 6 November 2024
4F-Trp labeled Oscillatoria Agardhii Agglutinin (OAA)4F-Trp labeled Oscillatoria Agardhii Agglutinin (OAA)
Structural highlights
FunctionPublication Abstract from PubMedTraditional protein structure determination by magic angle spinning (MAS) solid-state NMR spectroscopy primarily relies on interatomic distances up to 8 A, extracted from (13)C-, (15)N-, and (1)H-based dipolar-based correlation experiments. Here, we show that (19)F fast (60 kHz) MAS NMR spectroscopy can supply additional, longer distances. Using 4F-Trp,U-(13)C,(15)N crystalline Oscillatoria agardhii agglutinin (OAA), we demonstrate that judiciously designed 2D and 3D (19)F-based dipolar correlation experiments such as (H)CF, (H)CHF, and FF can yield interatomic distances in the 8-16 A range. Incorporation of fluorine-based restraints into structure calculation improved the precision of Trp side chain conformations as well as regions in the protein around the fluorine containing residues, with notable improvements observed for residues in proximity to the Trp pairs (W10/W17 and W77/W84) in the carbohydrate-binding loops, which lacked sufficient long-range (13)C-(13)C distance restraints. Our work highlights the use of fluorine and (19)F fast MAS NMR spectroscopy as a powerful structural biology tool. Integrating (19)F Distance Restraints for Accurate Protein Structure Determination by Magic Angle Spinning NMR Spectroscopy.,Runge BR, Zadorozhnyi R, Quinn CM, Russell RW, Lu M, Antolinez S, Struppe J, Schwieters CD, Byeon IL, Hadden-Perilla JA, Gronenborn AM, Polenova T J Am Chem Soc. 2024 Oct 23. doi: 10.1021/jacs.4c11373. PMID:39440810[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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