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| | <StructureSection load='2bej' size='340' side='right'caption='[[2bej]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2bej' size='340' side='right'caption='[[2bej]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BEJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BEJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vz0|1vz0]], [[1wcv|1wcv]], [[2bek|2bek]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=2bej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bej OCA], [https://pdbe.org/2bej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bej RCSB], [https://www.ebi.ac.uk/pdbsum/2bej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bej 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=2bej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bej OCA], [https://pdbe.org/2bej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bej RCSB], [https://www.ebi.ac.uk/pdbsum/2bej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bej ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SOJ_THET2 SOJ_THET2]] ATPase probably involved in chromosome partitioning. Cooperatively binds dsDNA, forming nucleoprotein filaments in a strictly ATP-dependent fashion. Can also bind ssDNA with lower affinity.<ref>PMID:15635448</ref>
| + | [https://www.uniprot.org/uniprot/SOJ_THET2 SOJ_THET2] ATPase probably involved in chromosome partitioning. Cooperatively binds dsDNA, forming nucleoprotein filaments in a strictly ATP-dependent fashion. Can also bind ssDNA with lower affinity.<ref>PMID:15635448</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet2]] | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Butler, P J.G]] | + | [[Category: Butler PJG]] |
| - | [[Category: Leonard, T A]] | + | [[Category: Leonard TA]] |
| - | [[Category: Lowe, J]] | + | [[Category: Lowe J]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Bacterial]]
| + | |
| - | [[Category: Chromosome segregation]]
| + | |
| - | [[Category: Soj]]
| + | |
| Structural highlights
Function
SOJ_THET2 ATPase probably involved in chromosome partitioning. Cooperatively binds dsDNA, forming nucleoprotein filaments in a strictly ATP-dependent fashion. Can also bind ssDNA with lower affinity.[1]
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
Soj and Spo0J of the Gram-negative hyperthermophile Thermus thermophilus belong to the conserved ParAB family of bacterial proteins implicated in plasmid and chromosome partitioning. Spo0J binds to DNA near the replication origin and localises at the poles following initiation of replication. Soj oscillates in the nucleoid region in an ATP- and Spo0J-dependent fashion. Here, we show that Soj undergoes ATP-dependent dimerisation in solution and forms nucleoprotein filaments with DNA. Crystal structures of Soj in three nucleotide states demonstrate that the empty and ADP-bound states are monomeric, while a hydrolysis-deficient mutant, D44A, is capable of forming a nucleotide 'sandwich' dimer. Soj ATPase activity is stimulated by Spo0J or the N-terminal 20 amino-acid peptide of Spo0J. Our analysis shows that dimerisation and activation involving a peptide containing a Lys/Arg is conserved for Soj, ParA and MinD and their modulators Spo0J, ParB and MinE, respectively. By homology to the nitrogenase iron protein and the GTPases Ffh/FtsY, we suggest that Soj dimerisation and regulation represent a conserved biological switch.
Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch.,Leonard TA, Butler PJ, Lowe J EMBO J. 2005 Jan 26;24(2):270-82. Epub 2005 Jan 6. PMID:15635448[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leonard TA, Butler PJ, Lowe J. Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch. EMBO J. 2005 Jan 26;24(2):270-82. Epub 2005 Jan 6. PMID:15635448
- ↑ Leonard TA, Butler PJ, Lowe J. Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch. EMBO J. 2005 Jan 26;24(2):270-82. Epub 2005 Jan 6. PMID:15635448
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