2bej: Difference between revisions
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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 [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2bej]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BEJ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vz0|1vz0]], [[1wcv|1wcv]], [[2bek|2bek]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vz0|1vz0]], [[1wcv|1wcv]], [[2bek|2bek]]</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=2bej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bej RCSB], [http://www.ebi.ac.uk/pdbsum/2bej PDBsum]</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=2bej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bej OCA], [http://pdbe.org/2bej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bej RCSB], [http://www.ebi.ac.uk/pdbsum/2bej PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2bej" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Thet2]] | ||
[[Category: Butler, P J.G]] | [[Category: Butler, P J.G]] | ||
[[Category: Leonard, T A]] | [[Category: Leonard, T A]] | ||
Revision as of 08:34, 10 September 2015
STRUCTURE OF THE BACTERIAL CHROMOSOME SEGREGATION PROTEIN SOJSTRUCTURE OF THE BACTERIAL CHROMOSOME SEGREGATION PROTEIN 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 PubMedSoj 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
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