4tps

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==Sporulation Inhibitor of DNA Replication, SirA, in complex with Domain I of DnaA==
==Sporulation Inhibitor of DNA Replication, SirA, in complex with Domain I of DnaA==
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<StructureSection load='4tps' size='340' side='right' caption='[[4tps]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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<StructureSection load='4tps' size='340' side='right'caption='[[4tps]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4tps]] is a 4 chain structure. 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>
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<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>
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</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>
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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]] 1.65&#8491;</td></tr>
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<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://www.rcsb.org/pdb/explore.do?structureId=4tps RCSB], [http://www.ebi.ac.uk/pdbsum/4tps PDBsum]</span></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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=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>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:25041308</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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==See Also==
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</div>
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*[[DnaA|DnaA]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fogg, M J]]
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
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[[Category: Grahl, A]]
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[[Category: Large Structures]]
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[[Category: Jameson, K H]]
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[[Category: Fogg MJ]]
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[[Category: Turkenburg, J P]]
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[[Category: Grahl A]]
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[[Category: Wilkinson, A J]]
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[[Category: Jameson KH]]
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[[Category: Inhibitory complex]]
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[[Category: Turkenburg JP]]
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[[Category: Replication]]
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[[Category: Wilkinson AJ]]
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[[Category: Sporulation]]
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Current revision

Sporulation Inhibitor of DNA Replication, SirA, in complex with Domain I of DnaA

PDB ID 4tps

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