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| - | [[Image:1qlk.jpg|left|200px]]<br /><applet load="1qlk" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1qlk" /> | |
| - | '''SOLUTION STRUCTURE OF CA(2+)-LOADED RAT S100B (BETABETA) NMR, 20 STRUCTURES'''<br /> | |
| | | | |
| - | ==Overview== | + | ==SOLUTION STRUCTURE OF CA(2+)-LOADED RAT S100B (BETABETA) NMR, 20 STRUCTURES== |
| - | The three-dimensional structure of Ca2+-bound rat S100B(betabeta) has been, determined using data from a series of two-dimensional (2D), three-dimensional (3D), and four-dimensional (4D) nuclear magnetic, resonance (NMR) experiments. Each S100beta subunit (91 residues) contains, four helixes (helix 1, E2-R20; helix 2, K29-N38; helix 3, Q50-D61; and, helix 4, F70-A83) and one antiparallel beta-sheet (strand 1, K26-K28; and, strand 2, E67-D69) which brings the normal and pseudo EF-hands together., As found previously for rat apo-S100B(betabeta) [Drohat, A. C., et al., (1996) Biochemistry 35, 11577-11588], helixes 1, 1', 4, and 4' associate, to form an X-type four-helix bundle at the symmetric dimer interface., Additionally, Ca2+ binding does not significantly change the interhelical, angle of helixes 1 and 2 in the pseudo EF-hand (apo, Omega1-2 = 132 +/- 4, degrees; and Ca2+-bound, Omega1-2 = 137 +/- 5 degrees). However, the, interhelical angle of helixes 3 and 4 in the normal EF-hand (Omega3-4 =, 106 +/- 4 degrees) changed significantly upon the addition of Ca2+, (DeltaOmega3-4 = 112 +/- 5 degrees) and is similar to that of the, Ca2+-bound EF-hands in calbindin D9K, calmodulin, and troponin (84 degrees, </= Omega </= 128 degrees). Further, the four helixes within each S100beta, subunit form a splayed-type four-helix bundle (four perpendicular helixes), as observed in Ca2+-bound calbindin D9K. The large Ca2+-dependent, conformational change involving helix 3 exposes a cleft, defined by, residues in the hinge region, the C-terminal loop, and helix 3, which is, absent in the apo structure. This surface on Ca2+-bound S100B(betabeta) is, likely important for target protein binding. | + | <StructureSection load='1qlk' size='340' side='right'caption='[[1qlk]]' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1qlk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QLK FirstGlance]. <br> |
| | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1qlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qlk OCA], [https://pdbe.org/1qlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qlk RCSB], [https://www.ebi.ac.uk/pdbsum/1qlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qlk ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/S100B_RAT S100B_RAT] 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. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:19910580</ref> <ref>PMID:20351179</ref> |
| | + | == 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/ql/1qlk_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=1qlk ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | The three-dimensional structure of Ca2+-bound rat S100B(betabeta) has been determined using data from a series of two-dimensional (2D), three-dimensional (3D), and four-dimensional (4D) nuclear magnetic resonance (NMR) experiments. Each S100beta subunit (91 residues) contains four helixes (helix 1, E2-R20; helix 2, K29-N38; helix 3, Q50-D61; and helix 4, F70-A83) and one antiparallel beta-sheet (strand 1, K26-K28; and strand 2, E67-D69) which brings the normal and pseudo EF-hands together. As found previously for rat apo-S100B(betabeta) [Drohat, A. C., et al. (1996) Biochemistry 35, 11577-11588], helixes 1, 1', 4, and 4' associate to form an X-type four-helix bundle at the symmetric dimer interface. Additionally, Ca2+ binding does not significantly change the interhelical angle of helixes 1 and 2 in the pseudo EF-hand (apo, Omega1-2 = 132 +/- 4 degrees; and Ca2+-bound, Omega1-2 = 137 +/- 5 degrees). However, the interhelical angle of helixes 3 and 4 in the normal EF-hand (Omega3-4 = 106 +/- 4 degrees) changed significantly upon the addition of Ca2+ (DeltaOmega3-4 = 112 +/- 5 degrees) and is similar to that of the Ca2+-bound EF-hands in calbindin D9K, calmodulin, and troponin (84 degrees </= Omega </= 128 degrees). Further, the four helixes within each S100beta subunit form a splayed-type four-helix bundle (four perpendicular helixes) as observed in Ca2+-bound calbindin D9K. The large Ca2+-dependent conformational change involving helix 3 exposes a cleft, defined by residues in the hinge region, the C-terminal loop, and helix 3, which is absent in the apo structure. This surface on Ca2+-bound S100B(betabeta) is likely important for target protein binding. |
| | | | |
| - | ==About this Structure==
| + | Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,.,Drohat AC, Baldisseri DM, Rustandi RR, Weber DJ Biochemistry. 1998 Mar 3;37(9):2729-40. PMID:9485423<ref>PMID:9485423</ref> |
| - | 1QLK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QLK OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,., Drohat AC, Baldisseri DM, Rustandi RR, Weber DJ, Biochemistry. 1998 Mar 3;37(9):2729-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9485423 9485423]
| + | </div> |
| - | [[Category: Rattus norvegicus]]
| + | <div class="pdbe-citations 1qlk" style="background-color:#fffaf0;"></div> |
| - | [[Category: Single protein]]
| + | |
| - | [[Category: Baldisseri, D.M.]]
| + | |
| - | [[Category: Drohat, A.C.]]
| + | |
| - | [[Category: Rustandi, R.R.]]
| + | |
| - | [[Category: Weber, D.J.]]
| + | |
| - | [[Category: CA]]
| + | |
| - | [[Category: calcium-binding protein]]
| + | |
| - | [[Category: ef-hand]]
| + | |
| - | [[Category: four-helix bundle]]
| + | |
| - | [[Category: nmr]]
| + | |
| - | [[Category: s100 protein]]
| + | |
| - | [[Category: s100b]]
| + | |
| - | [[Category: s100beta]]
| + | |
| | | | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:47:47 2007''
| + | ==See Also== |
| | + | *[[S100 proteins 3D structures|S100 proteins 3D structures]] |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | + | [[Category: Rattus norvegicus]] |
| | + | [[Category: Baldisseri DM]] |
| | + | [[Category: Drohat AC]] |
| | + | [[Category: Rustandi RR]] |
| | + | [[Category: Weber DJ]] |
| Structural highlights
Function
S100B_RAT 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. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of Ca2+-bound rat S100B(betabeta) has been determined using data from a series of two-dimensional (2D), three-dimensional (3D), and four-dimensional (4D) nuclear magnetic resonance (NMR) experiments. Each S100beta subunit (91 residues) contains four helixes (helix 1, E2-R20; helix 2, K29-N38; helix 3, Q50-D61; and helix 4, F70-A83) and one antiparallel beta-sheet (strand 1, K26-K28; and strand 2, E67-D69) which brings the normal and pseudo EF-hands together. As found previously for rat apo-S100B(betabeta) [Drohat, A. C., et al. (1996) Biochemistry 35, 11577-11588], helixes 1, 1', 4, and 4' associate to form an X-type four-helix bundle at the symmetric dimer interface. Additionally, Ca2+ binding does not significantly change the interhelical angle of helixes 1 and 2 in the pseudo EF-hand (apo, Omega1-2 = 132 +/- 4 degrees; and Ca2+-bound, Omega1-2 = 137 +/- 5 degrees). However, the interhelical angle of helixes 3 and 4 in the normal EF-hand (Omega3-4 = 106 +/- 4 degrees) changed significantly upon the addition of Ca2+ (DeltaOmega3-4 = 112 +/- 5 degrees) and is similar to that of the Ca2+-bound EF-hands in calbindin D9K, calmodulin, and troponin (84 degrees </= Omega </= 128 degrees). Further, the four helixes within each S100beta subunit form a splayed-type four-helix bundle (four perpendicular helixes) as observed in Ca2+-bound calbindin D9K. The large Ca2+-dependent conformational change involving helix 3 exposes a cleft, defined by residues in the hinge region, the C-terminal loop, and helix 3, which is absent in the apo structure. This surface on Ca2+-bound S100B(betabeta) is likely important for target protein binding.
Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,.,Drohat AC, Baldisseri DM, Rustandi RR, Weber DJ Biochemistry. 1998 Mar 3;37(9):2729-40. PMID:9485423[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tsoporis JN, Izhar S, Leong-Poi H, Desjardins JF, Huttunen HJ, Parker TG. S100B interaction with the receptor for advanced glycation end products (RAGE): a novel receptor-mediated mechanism for myocyte apoptosis postinfarction. Circ Res. 2010 Jan 8;106(1):93-101. doi: 10.1161/CIRCRESAHA.109.195834. Epub 2009, Nov 12. PMID:19910580 doi:10.1161/CIRCRESAHA.109.195834
- ↑ Gilquin B, Cannon BR, Hubstenberger A, Moulouel B, Falk E, Merle N, Assard N, Kieffer S, Rousseau D, Wilder PT, Weber DJ, Baudier J. The calcium-dependent interaction between S100B and the mitochondrial AAA ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A. Mol Cell Biol. 2010 Jun;30(11):2724-36. doi: 10.1128/MCB.01468-09. Epub 2010 Mar , 29. PMID:20351179 doi:10.1128/MCB.01468-09
- ↑ Drohat AC, Baldisseri DM, Rustandi RR, Weber DJ. Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,. Biochemistry. 1998 Mar 3;37(9):2729-40. PMID:9485423 doi:10.1021/bi972635p
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