2c41

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[[Image:2c41.gif|left|200px]]<br />
 
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<applet load="2c41" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c41, resolution 1.81&Aring;" />
 
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'''X-RAY STRUCTURE OF DPS FROM THERMOSYNECHOCOCCUS ELONGATUS'''<br />
 
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==Overview==
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==X-ray structure of Dps from Thermosynechococcus elongatus==
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DNA-binding proteins from starved cells (Dps proteins) protect bacteria, primarily from oxidative damage. They are composed of 12 identical, subunits assembled with 23-symmetry to form a compact cage-like structure, known to be stable at temperatures &gt; 70 degrees C and over a wide pH, range. Thermosynechococcus elongatus Dps thermostability is increased, dramatically relative to mesophilic Dps proteins. Hydrophobic interactions, at the dimeric and trimeric interfaces called Dps-like are replaced by, salt bridges and hydrogen bonds, a common strategy in thermophiles., Moreover, the buried surface area at the least-extended Dps-like interface, is significantly increased. A peculiarity of T. elongatus Dps is the, presence of a chloride ion coordinated with threefold symmetry-related, arginine residues lining the opening of the Dps-like pore toward the, internal cavity. T. elongatus Dps conserves the unusual intersubunit, ferroxidase centre that allows the Dps protein family to oxidize Fe(II), with hydrogen peroxide, thereby inhibiting free radical production via, Fenton chemistry. This catalytic property is of special importance in T., elongatus (which lacks the catalase gene) in the protection of DNA and, photosystems I and II from hydrogen peroxide-mediated oxidative damage.
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<StructureSection load='2c41' size='340' side='right'caption='[[2c41]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c41]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C41 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=2c41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c41 OCA], [https://pdbe.org/2c41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c41 RCSB], [https://www.ebi.ac.uk/pdbsum/2c41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c41 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8DG54_THEVB Q8DG54_THEVB]
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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/c4/2c41_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=2c41 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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DNA-binding proteins from starved cells (Dps proteins) protect bacteria primarily from oxidative damage. They are composed of 12 identical subunits assembled with 23-symmetry to form a compact cage-like structure known to be stable at temperatures &gt; 70 degrees C and over a wide pH range. Thermosynechococcus elongatus Dps thermostability is increased dramatically relative to mesophilic Dps proteins. Hydrophobic interactions at the dimeric and trimeric interfaces called Dps-like are replaced by salt bridges and hydrogen bonds, a common strategy in thermophiles. Moreover, the buried surface area at the least-extended Dps-like interface is significantly increased. A peculiarity of T. elongatus Dps is the presence of a chloride ion coordinated with threefold symmetry-related arginine residues lining the opening of the Dps-like pore toward the internal cavity. T. elongatus Dps conserves the unusual intersubunit ferroxidase centre that allows the Dps protein family to oxidize Fe(II) with hydrogen peroxide, thereby inhibiting free radical production via Fenton chemistry. This catalytic property is of special importance in T. elongatus (which lacks the catalase gene) in the protection of DNA and photosystems I and II from hydrogen peroxide-mediated oxidative damage.
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==About this Structure==
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Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus.,Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A FEBS J. 2006 Nov;273(21):4913-28. Epub 2006 Oct 3. PMID:17018059<ref>PMID:17018059</ref>
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2C41 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermosynechococcus_elongatus Thermosynechococcus elongatus] with CL, PG4 and PGE as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C41 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus., Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A, FEBS J. 2006 Nov;273(21):4913-28. Epub 2006 Oct 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17018059 17018059]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2c41" style="background-color:#fffaf0;"></div>
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[[Category: Thermosynechococcus elongatus]]
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== References ==
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[[Category: Ceci, P.]]
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<references/>
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[[Category: Chiancone, E.]]
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__TOC__
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[[Category: Franceschini, S.]]
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</StructureSection>
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[[Category: Ilari, A.]]
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[[Category: Large Structures]]
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[[Category: CL]]
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[[Category: Thermosynechococcus vestitus BP-1]]
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[[Category: PG4]]
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[[Category: Ceci P]]
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[[Category: PGE]]
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[[Category: Chiancone E]]
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[[Category: dna-binding protein]]
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[[Category: Franceschini S]]
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[[Category: dps (dna-binding proteins from starved cells)]]
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[[Category: Ilari A]]
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[[Category: iron binding]]
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[[Category: iron-binding/oxidation protein]]
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[[Category: stress protein]]
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[[Category: thermophilic cyanobacterium]]
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[[Category: thermostable protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:58:01 2007''
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Current revision

X-ray structure of Dps from Thermosynechococcus elongatus

PDB ID 2c41

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