3c21

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{{Seed}}
 
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[[Image:3c21.png|left|200px]]
 
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==Structure of a bacterial DNA damage sensor protein with reaction product==
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The line below this paragraph, containing "STRUCTURE_3c21", creates the "Structure Box" on the page.
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<StructureSection load='3c21' size='340' side='right'caption='[[3c21]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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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'>[[3c21]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C21 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]] 2.7&#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=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene></td></tr>
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{{STRUCTURE_3c21| PDB=3c21 | 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=3c21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c21 OCA], [https://pdbe.org/3c21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c21 RCSB], [https://www.ebi.ac.uk/pdbsum/3c21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c21 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DISA_THEMA DISA_THEMA] Participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions (By similarity).<ref>PMID:18439896</ref> Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. Does not convert GTP to c-di-GMP.<ref>PMID:18439896</ref>
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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/c2/3c21_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=3c21 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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To reveal mechanisms of DNA damage checkpoint initiation, we structurally and biochemically analyzed DisA, a protein that controls a Bacillus subtilis sporulation checkpoint in response to DNA double-strand breaks. We find that DisA forms a large octamer that consists of an array of an uncharacterized type of nucleotide-binding domain along with two DNA-binding regions related to the Holliday junction recognition protein RuvA. Remarkably, the nucleotide-binding domains possess diadenylate cyclase activity. The resulting cyclic diadenosine phosphate, c-di-AMP, is reminiscent but distinct from c-di-GMP, an emerging prokaryotic regulator of complex cellular processes. Diadenylate cyclase activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions. Our data indicate that DisA signals DNA structures that interfere with chromosome segregation via c-di-AMP. Identification of the diadenylate cyclase domain in other eubacterial and archaeal proteins implies a more general role for c-di-AMP in prokaryotes.
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===Structure of a bacterial DNA damage sensor protein with reaction product===
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Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates.,Witte G, Hartung S, Buttner K, Hopfner KP Mol Cell. 2008 Apr 25;30(2):167-78. PMID:18439896<ref>PMID:18439896</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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The line below this paragraph, {{ABSTRACT_PUBMED_18439896}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3c21" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18439896 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18439896}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3C21 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C21 OCA].
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==Reference==
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Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates., Witte G, Hartung S, Buttner K, Hopfner KP, Mol Cell. 2008 Apr 25;30(2):167-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18439896 18439896]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Buttner, K.]]
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[[Category: Buttner K]]
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[[Category: Hartung, S.]]
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[[Category: Hartung S]]
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[[Category: Hopfner, K P.]]
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[[Category: Hopfner KP]]
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[[Category: Witte, G.]]
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[[Category: Witte G]]
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[[Category: Dna binding protein]]
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[[Category: Dna damage]]
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[[Category: Dna repair]]
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[[Category: Dna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:53:25 2008''
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Current revision

Structure of a bacterial DNA damage sensor protein with reaction product

PDB ID 3c21

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