2jpt

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{{Seed}}
 
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[[Image:2jpt.png|left|200px]]
 
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==Structural changes induced in apo-s100a1 protein by the disulphide formation between its CYS85 residue and b-mercaptoethanol==
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The line below this paragraph, containing "STRUCTURE_2jpt", creates the "Structure Box" on the page.
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<StructureSection load='2jpt' size='340' side='right'caption='[[2jpt]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jpt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JPT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
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{{STRUCTURE_2jpt| PDB=2jpt | SCENE= }}
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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=2jpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpt OCA], [https://pdbe.org/2jpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jpt RCSB], [https://www.ebi.ac.uk/pdbsum/2jpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jpt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/S10A1_BOVIN S10A1_BOVIN] 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jp/2jpt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2jpt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recently, we have shown (Goch, G., Vdovenko, S., Kozlowska, H., and Bierzynski, A. (2005) FEBS J. 272, 2557-2565) that the chemical modification of Cys 85 residue of S100A1 protein by disulfide bond formation with small thiols such as glutathione, cysteine, or beta-mercaptoethanol (betaME) leads to a dramatic increase of the protein affinity for calcium. Therefore, the biological function of S100A1 as a calcium signal transmitter is probably regulated by the redox potential within the cell. Systematic, structural studies of various mixed disulfides of S100A1 in the apo and holo states are necessary to elucidate the mechanism of this phenomenon. Using NMR methods we have determined the structure of apo-S100A1-betaME and, on the basis of 15N nuclear magnetic relaxation data, we have characterized the structural dynamics of both: modified and unmodified molecules of apo-S100A1. The following effects of betaME modification have been observed: (1) Helices IV and IV' of two protein subunits are elongated by five residues (85-89). (2) Conformation of the calcium binding N-terminal loops is dramatically changed, and structural flexibility of the N-loops as well as C-loops markedly increases. (3) The angle between helices I and IV increases by approximately 20 degrees and between helices IV and IV' decreases by approximately 35 degrees . All these observations lead to the conclusion that betaME modification of apo-S100A1 makes its structure more similar to that of holo-S100A1, so that it becomes much better adjusted for calcium coordination.
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===Structural changes induced in apo-s100a1 protein by the disulphide formation between its CYS85 residue and b-mercaptoethanol===
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Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol.,Zhukov I, Ejchart A, Bierzynski A Biochemistry. 2008 Jan 15;47(2):640-50. Epub 2007 Dec 19. PMID:18088104<ref>PMID:18088104</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2jpt" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18088104}}, adds the Publication Abstract to the page
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*[[S100 proteins 3D structures|S100 proteins 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18088104 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18088104}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2JPT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPT OCA].
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==Reference==
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Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol., Zhukov I, Ejchart A, Bierzynski A, Biochemistry. 2008 Jan 15;47(2):640-50. Epub 2007 Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18088104 18088104]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bierzynski, A.]]
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[[Category: Bierzynski A]]
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[[Category: Ejchart, A.]]
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[[Category: Ejchart A]]
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[[Category: Zhukov, I.]]
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[[Category: Zhukov I]]
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[[Category: B-mercaptoethanol]]
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[[Category: Metal binding protein]]
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[[Category: Mixed disulfide]]
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[[Category: S100 protein]]
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[[Category: S100a1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:44:03 2008''
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Current revision

Structural changes induced in apo-s100a1 protein by the disulphide formation between its CYS85 residue and b-mercaptoethanol

PDB ID 2jpt

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