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| | ==NMR solution structure of staphylococcal protein A, C domain== | | ==NMR solution structure of staphylococcal protein A, C domain== |
| - | <StructureSection load='6sow' size='340' side='right'caption='[[6sow]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6sow' size='340' side='right'caption='[[6sow]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sow]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SOW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sow]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SOW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spa ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=6sow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sow OCA], [https://pdbe.org/6sow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sow RCSB], [https://www.ebi.ac.uk/pdbsum/6sow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sow 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=6sow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sow OCA], [https://pdbe.org/6sow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sow RCSB], [https://www.ebi.ac.uk/pdbsum/6sow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sow ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SPA_STAA8 SPA_STAA8] |
| | <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: Backlund, S M]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Iwai, H]] | + | [[Category: Backlund SM]] |
| - | [[Category: Immune system]] | + | [[Category: Iwai H]] |
| - | [[Category: Immunoglobulin-binding protein]]
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| - | [[Category: Protein binding]]
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| - | [[Category: Three-helix bundle]]
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| Structural highlights
Function
SPA_STAA8
Publication Abstract from PubMed
Uniformly (13)C- and (15)N-labeled samples ensure fast and reliable nuclear magnetic resonance (NMR) assignments of proteins and are commonly used for structure elucidation by NMR. However, the preparation of uniformly labeled samples is a labor-intensive and expensive step. Reducing the portion of (13)C-labeled glucose by a factor of five using a fractional 20% (13)C- and 100% (15)N-labeling scheme could lower the total chemical costs, yet retaining sufficient structural information of uniformly [(13)C, (15)N]-labeled sample as a result of the improved sensitivity of NMR instruments. Moreover, fractional (13)C-labeling can facilitate reliable resonance assignments of sidechains because of the biosynthetic pathways of each amino-acid. Preparation of only one [20% (13)C, 100% (15)N]-labeled sample for small proteins (<15 kDa) could also eliminate redundant sample preparations of 100% (15)N-labeled and uniformly 100% [(13)C, (15)N]-labeled samples of proteins. We determined the NMR structures of a small alpha-helical protein, the C domain of IgG-binding protein A from Staphylococcus aureus (SpaC), and a small beta-sheet protein, CBM64 module using [20% (13)C, 100% (15)N]-labeled sample and compared with the crystal structures and the NMR structures derived from the 100% [(13)C, (15)N]-labeled sample. Our results suggest that one [20% (13)C, 100% (15)N]-labeled sample of small proteins could be routinely used as an alternative to conventional 100% [(13)C, (15)N]-labeling for backbone resonance assignments, NMR structure determination, (15)N-relaxation analysis, and ligand-protein interaction.
NMR Structure Determinations of Small Proteins Using only One Fractionally 20% (13)C- and Uniformly 100% (15)N-Labeled Sample.,Heikkinen HA, Backlund SM, Iwai H Molecules. 2021 Feb 1;26(3). pii: molecules26030747. doi:, 10.3390/molecules26030747. PMID:33535444[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Heikkinen HA, Backlund SM, Iwai H. NMR Structure Determinations of Small Proteins Using only One Fractionally 20% (13)C- and Uniformly 100% (15)N-Labeled Sample. Molecules. 2021 Feb 1;26(3). pii: molecules26030747. doi:, 10.3390/molecules26030747. PMID:33535444 doi:http://dx.doi.org/10.3390/molecules26030747
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