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| | <StructureSection load='1se8' size='340' side='right'caption='[[1se8]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1se8' size='340' side='right'caption='[[1se8]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1se8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SE8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SE8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1se8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SE8 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSB, DR0099 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 "Micrococcus radiodurans" Raj et al. 1960])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1se8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1se8 OCA], [http://pdbe.org/1se8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1se8 RCSB], [http://www.ebi.ac.uk/pdbsum/1se8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1se8 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=1se8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1se8 OCA], [https://pdbe.org/1se8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1se8 RCSB], [https://www.ebi.ac.uk/pdbsum/1se8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1se8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SSB_DEIRA SSB_DEIRA]] This protein is essential for replication of the chromosome. It is also involved in DNA recombination and repair (By similarity). | + | [https://www.uniprot.org/uniprot/SSB_DEIRA SSB_DEIRA] This protein is essential for replication of the chromosome. It is also involved in DNA recombination and repair (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/se/1se8_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/se/1se8_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micrococcus radiodurans raj et al. 1960]] | + | [[Category: Deinococcus radiodurans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bernstein, D A]] | + | [[Category: Bernstein DA]] |
| - | [[Category: Cox, M M]] | + | [[Category: Cox MM]] |
| - | [[Category: Eggington, J M]] | + | [[Category: Eggington JM]] |
| - | [[Category: Keck, J L]] | + | [[Category: Keck JL]] |
| - | [[Category: Killoran, M P]] | + | [[Category: Killoran MP]] |
| - | [[Category: Misic, A M]] | + | [[Category: Misic AM]] |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Single-strand binding protein]]
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| Structural highlights
Function
SSB_DEIRA This protein is essential for replication of the chromosome. It is also involved in DNA recombination and repair (By similarity).
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
Single-stranded DNA (ssDNA)-binding (SSB) proteins are uniformly required to bind and protect single-stranded intermediates in DNA metabolic pathways. All bacterial and eukaryotic SSB proteins studied to date oligomerize to assemble four copies of a conserved domain, called an oligonucleotide/oligosaccharide-binding (OB) fold, that cooperate in nonspecific ssDNA binding. The vast majority of bacterial SSB family members function as homotetramers, with each monomer contributing a single OB fold. However, SSB proteins from the Deinococcus-Thermus genera are exceptions to this rule, because they contain two OB folds per monomer. To investigate the structural consequences of this unusual arrangement, we have determined a 1.8-A-resolution x-ray structure of Deinococcus radiodurans SSB. The structure shows that D. radiodurans SSB comprises two OB domains linked by a beta-hairpin motif. The protein assembles a four-OB-fold arrangement by means of symmetric dimerization. In contrast to homotetrameric SSB proteins, asymmetry exists between the two OB folds of D. radiodurans SSB because of sequence differences between the domains. These differences appear to reflect specialized roles that have evolved for each domain. Extensive crystallographic contacts link D. radiodurans SSB dimers in an arrangement that has important implications for higher-order structures of the protein bound to ssDNA. This assembly utilizes the N-terminal OB domain and the beta-hairpin structure that is unique to Deinococcus and Thermus species SSB proteins. We hypothesize that differences between D. radiodurans SSB and homotetrameric bacterial SSB proteins may confer a selective advantage to D. radiodurans cells that aids viability in environments that challenge genomic stability.
Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage.,Bernstein DA, Eggington JM, Killoran MP, Misic AM, Cox MM, Keck JL Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8575-80. Epub 2004 May 24. PMID:15159541[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bernstein DA, Eggington JM, Killoran MP, Misic AM, Cox MM, Keck JL. Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage. Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8575-80. Epub 2004 May 24. PMID:15159541 doi:10.1073/pnas.0401331101
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