7dv3: Difference between revisions
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==Structure of Sulfolobus solfataricus SegA-AMPPNP protein== | |||
<StructureSection load='7dv3' size='340' side='right'caption='[[7dv3]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7dv3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DV3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7dv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dv3 OCA], [https://pdbe.org/7dv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dv3 RCSB], [https://www.ebi.ac.uk/pdbsum/7dv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dv3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q981B3_SACS2 Q981B3_SACS2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Genome segregation is a vital process in all organisms. Chromosome partitioning remains obscure in Archaea, the third domain of life. Here, we investigated the SegAB system from Sulfolobus solfataricus. SegA is a ParA Walker-type ATPase and SegB is a site-specific DNA-binding protein. We determined the structures of both proteins and those of SegA-DNA and SegB-DNA complexes. The SegA structure revealed an atypical, novel non-sandwich dimer that binds DNA either in the presence or in the absence of ATP. The SegB structure disclosed a ribbon-helix-helix motif through which the protein binds DNA site specifically. The association of multiple interacting SegB dimers with the DNA results in a higher order chromatin-like structure. The unstructured SegB N-terminus plays an essential catalytic role in stimulating SegA ATPase activity and an architectural regulatory role in segrosome (SegA-SegB-DNA) formation. Electron microscopy results also provide a compact ring-like segrosome structure related to chromosome organization. These findings contribute a novel mechanistic perspective on archaeal chromosome segregation. | |||
Chromosome segregation in Archaea: SegA- and SegB-DNA complex structures provide insights into segrosome assembly.,Yen CY, Lin MG, Chen BW, Ng IW, Read N, Kabli AF, Wu CT, Shen YY, Chen CH, Barilla D, Sun YJ, Hsiao CD Nucleic Acids Res. 2021 Dec 16;49(22):13150-13164. doi: 10.1093/nar/gkab1155. PMID:34850144<ref>PMID:34850144</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7dv3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharolobus solfataricus P2]] | |||
[[Category: Hsiao CD]] | |||
[[Category: Lin MG]] | |||
[[Category: Sun YJ]] | |||
[[Category: Wu CT]] | |||
[[Category: Yen CY]] | |||
Latest revision as of 19:39, 29 November 2023
Structure of Sulfolobus solfataricus SegA-AMPPNP proteinStructure of Sulfolobus solfataricus SegA-AMPPNP protein
Structural highlights
FunctionPublication Abstract from PubMedGenome segregation is a vital process in all organisms. Chromosome partitioning remains obscure in Archaea, the third domain of life. Here, we investigated the SegAB system from Sulfolobus solfataricus. SegA is a ParA Walker-type ATPase and SegB is a site-specific DNA-binding protein. We determined the structures of both proteins and those of SegA-DNA and SegB-DNA complexes. The SegA structure revealed an atypical, novel non-sandwich dimer that binds DNA either in the presence or in the absence of ATP. The SegB structure disclosed a ribbon-helix-helix motif through which the protein binds DNA site specifically. The association of multiple interacting SegB dimers with the DNA results in a higher order chromatin-like structure. The unstructured SegB N-terminus plays an essential catalytic role in stimulating SegA ATPase activity and an architectural regulatory role in segrosome (SegA-SegB-DNA) formation. Electron microscopy results also provide a compact ring-like segrosome structure related to chromosome organization. These findings contribute a novel mechanistic perspective on archaeal chromosome segregation. Chromosome segregation in Archaea: SegA- and SegB-DNA complex structures provide insights into segrosome assembly.,Yen CY, Lin MG, Chen BW, Ng IW, Read N, Kabli AF, Wu CT, Shen YY, Chen CH, Barilla D, Sun YJ, Hsiao CD Nucleic Acids Res. 2021 Dec 16;49(22):13150-13164. doi: 10.1093/nar/gkab1155. PMID:34850144[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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