3iku
From Proteopedia
(Difference between revisions)
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<SX load='3iku' size='340' side='right' viewer='molstar' caption='[[3iku]], [[Resolution|resolution]] 18.00Å' scene=''> | <SX load='3iku' size='340' side='right' viewer='molstar' caption='[[3iku]], [[Resolution|resolution]] 18.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3iku]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3iku]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IKU FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 18Å</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=3iku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iku OCA], [https://pdbe.org/3iku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iku RCSB], [https://www.ebi.ac.uk/pdbsum/3iku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iku 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=3iku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iku OCA], [https://pdbe.org/3iku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iku RCSB], [https://www.ebi.ac.uk/pdbsum/3iku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iku ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/PARM_ECOLX PARM_ECOLX] Involved in the control of plasmid partition. Required for the accurate segregation of the plasmid. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3iku ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3iku ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Segregation of the R1 plasmid in bacteria relies on ParM, an actin homolog that segregates plasmids by switching between cycles of polymerization and depolymerization. We find similar polymerization kinetics and stability in the presence of either ATP or GTP and a 10-fold affinity preference for ATP over GTP. We used electron cryo-microscopy to evaluate the heterogeneity within ParM filaments. In addition to variable twist, ParM has variable axial rise, and both parameters are coupled. Subunits in the same ParM filaments can exist in two different structural states, with the nucleotide-binding cleft closed or open, and the bound nucleotide biases the distribution of states. The interface between protomers is different between these states, and in neither state is it similar to F-actin. Our results suggest that the closed state of the cleft is required but not sufficient for ParM polymerization, and provide a structural basis for the dynamic instability of ParM filaments. | ||
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- | Structural polymorphism of the ParM filament and dynamic instability.,Galkin VE, Orlova A, Rivera C, Mullins RD, Egelman EH Structure. 2009 Sep 9;17(9):1253-64. PMID:19748346<ref>PMID:19748346</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3iku" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Plasmid segregation protein ParM|Plasmid segregation protein ParM]] | *[[Plasmid segregation protein ParM|Plasmid segregation protein ParM]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
- | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Egelman | + | [[Category: Egelman EH]] |
- | [[Category: Galkin | + | [[Category: Galkin VE]] |
- | [[Category: Mullins | + | [[Category: Mullins RD]] |
- | [[Category: Orlova | + | [[Category: Orlova A]] |
- | [[Category: Rivera | + | [[Category: Rivera C]] |
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Current revision
Structural model of ParM filament in closed state from cryo-EM
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