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| | <StructureSection load='4tps' size='340' side='right'caption='[[4tps]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='4tps' size='340' side='right'caption='[[4tps]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tps]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TPS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tps]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TPS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sirA, yneE, yoxF, BSU17900 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU]), dnaA, dnaH, BSU00010 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=4tps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tps OCA], [https://pdbe.org/4tps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tps RCSB], [https://www.ebi.ac.uk/pdbsum/4tps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tps ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tps OCA], [http://pdbe.org/4tps PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tps RCSB], [http://www.ebi.ac.uk/pdbsum/4tps PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tps ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SIRA_BACSU SIRA_BACSU]] Inhibits DNA replication in growing cells, thus reducing chromosome copy number and playing a significant role during the onset of sporulation. [[http://www.uniprot.org/uniprot/DNAA_BACSU DNAA_BACSU]] Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. DnaA can inhibit its own gene expression as well as that of other genes. | + | [https://www.uniprot.org/uniprot/SIRA_BACSU SIRA_BACSU] Inhibits DNA replication in growing cells, thus reducing chromosome copy number and playing a significant role during the onset of sporulation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4tps" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4tps" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[DnaA|DnaA]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fogg, M J]] | + | [[Category: Fogg MJ]] |
| - | [[Category: Grahl, A]] | + | [[Category: Grahl A]] |
| - | [[Category: Jameson, K H]] | + | [[Category: Jameson KH]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Wilkinson, A J]] | + | [[Category: Wilkinson AJ]] |
| - | [[Category: Inhibitory complex]]
| + | |
| - | [[Category: Replication]]
| + | |
| - | [[Category: Sporulation]]
| + | |
| Structural highlights
Function
SIRA_BACSU Inhibits DNA replication in growing cells, thus reducing chromosome copy number and playing a significant role during the onset of sporulation.
Publication Abstract from PubMed
Chromosome copy number in cells is controlled so that the frequency of initiation of DNA replication matches that of cell division. In bacteria, this is achieved through regulation of the interaction between the initiator protein DnaA and specific DNA elements arrayed at the origin of replication. DnaA assembles at the origin and promotes DNA unwinding and the assembly of a replication initiation complex. SirA is a DnaA-interacting protein that inhibits initiation of replication in diploid Bacillus subtilis cells committed to the developmental pathway leading to formation of a dormant spore. Here we present the crystal structure of SirA in complex with the N-terminal domain of DnaA revealing a heterodimeric complex. The interacting surfaces of both proteins are alpha-helical with predominantly apolar side chains packing in a hydrophobic interface. Site-directed mutagenesis experiments confirm the importance of this interface for the interaction of the two proteins in vitro and in vivo. Localization of GFP-SirA indicates that the protein accumulates at the replisome in sporulating cells, likely through a direct interaction with DnaA. The SirA interacting surface of DnaA corresponds closely to the HobA-interacting surface of DnaA from Helicobacter pylori even though HobA is an activator of DnaA and SirA is an inhibitor.
Structure and Interactions of the Bacillus subtilis Sporulation Inhibitor of DNA Replication, SirA, with Domain I of DnaA.,Jameson KH, Rostami N, Fogg MJ, Turkenburg JP, Grahl A, Murray H, Wilkinson AJ Mol Microbiol. 2014 Jul 11. doi: 10.1111/mmi.12713. PMID:25041308[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jameson KH, Rostami N, Fogg MJ, Turkenburg JP, Grahl A, Murray H, Wilkinson AJ. Structure and Interactions of the Bacillus subtilis Sporulation Inhibitor of DNA Replication, SirA, with Domain I of DnaA. Mol Microbiol. 2014 Jul 11. doi: 10.1111/mmi.12713. PMID:25041308 doi:http://dx.doi.org/10.1111/mmi.12713
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