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| | ==Post-translational S-nitrosylation is an endogenous factor fine-tuning human S100A1 protein properties== | | ==Post-translational S-nitrosylation is an endogenous factor fine-tuning human S100A1 protein properties== |
| - | <StructureSection load='2llt' size='340' side='right'caption='[[2llt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2llt' size='340' side='right'caption='[[2llt]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2llt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LLT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2llt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LLT FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2llu|2llu]]</div></td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100A1, S100A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2llt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2llt OCA], [https://pdbe.org/2llt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2llt RCSB], [https://www.ebi.ac.uk/pdbsum/2llt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2llt 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=2llt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2llt OCA], [https://pdbe.org/2llt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2llt RCSB], [https://www.ebi.ac.uk/pdbsum/2llt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2llt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/S10A1_HUMAN S10A1_HUMAN]] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites.
| + | [https://www.uniprot.org/uniprot/S10A1_HUMAN S10A1_HUMAN] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Poznanski, J]] | + | [[Category: Lenarcic Zivkovic M]] |
| - | [[Category: Wyslouch-Cieszynska, A]] | + | [[Category: Poznanski J]] |
| - | [[Category: Zareba-Koziol, M]] | + | [[Category: Wyslouch-Cieszynska A]] |
| - | [[Category: Zhukov, I]] | + | [[Category: Zareba-Koziol M]] |
| - | [[Category: Zhukova, L]] | + | [[Category: Zhukov I]] |
| - | [[Category: Zivkovic, M Lenarcic]]
| + | [[Category: Zhukova L]] |
| - | [[Category: Ca-binding protein]]
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| - | [[Category: Metal binding protein]]
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| - | [[Category: S-nitrosylation]]
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| Structural highlights
Function
S10A1_HUMAN Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites.
Publication Abstract from PubMed
S100A1 is a member of the Ca(2+)-binding S100 protein family. It is expressed in brain and heart tissue, where it plays a crucial role as a modulator of Ca(2+) homeostasis, energy metabolism, neurotransmitter release, and contractile performance. Biological effects of S100A1 have been attributed to its direct interaction with a variety of target proteins. The (patho)physiological relevance of S100A1 makes it an important molecular target for future therapeutic intervention. S-Nitrosylation is a post-translational modification of proteins, which plays a role in cellular signal transduction under physiological and pathological conditions. In this study, we confirmed that S100A1 protein is endogenously modified by Cys(85) S-nitrosylation in PC12 cells, which are a well established model system for studying S100A1 function. We used isothermal calorimetry to show that S-nitrosylation facilitates the formation of Ca(2+)-loaded S100A1 at physiological ionic strength conditions. To establish the unique influence of the S-nitroso group, our study describes high resolution three-dimensional structures of human apo-S100A1 protein with the Cys(85) thiol group in reduced and S-nitrosylated states. Solution structures of the proteins are based on NMR data obtained at physiological ionic strength. Comparative analysis shows that S-nitrosylation fine tunes the overall architecture of S100A1 protein. Although the typical S100 protein intersubunit four-helix bundle is conserved upon S-nitrosylation, the conformation of S100A1 protein is reorganized at the sites most important for target recognition (i.e. the C-terminal helix and the linker connecting two EF-hand domains). In summary, this study discloses cysteine S-nitrosylation as a new factor responsible for increasing functional diversity of S100A1 and helps explain the role of S100A1 as a Ca(2+) signal transmitter sensitive to NO/redox equilibrium within cells.
Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein.,Lenarcic Zivkovic M, Zareba-Koziol M, Zhukova L, Poznanski J, Zhukov I, Wyslouch-Cieszynska A J Biol Chem. 2012 Nov 23;287(48):40457-70. doi: 10.1074/jbc.M112.418392. Epub, 2012 Sep 18. PMID:22989881[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lenarcic Zivkovic M, Zareba-Koziol M, Zhukova L, Poznanski J, Zhukov I, Wyslouch-Cieszynska A. Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein. J Biol Chem. 2012 Nov 23;287(48):40457-70. doi: 10.1074/jbc.M112.418392. Epub, 2012 Sep 18. PMID:22989881 doi:http://dx.doi.org/10.1074/jbc.M112.418392
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