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| | <StructureSection load='2zgz' size='340' side='right'caption='[[2zgz]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='2zgz' size='340' side='right'caption='[[2zgz]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zgz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZGZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZGZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zgz]] is a 2 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=2ZGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZGZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</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]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zgy|2zgy]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</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'>[http://proteopedia.org/fgij/fg.htm?mol=2zgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zgz OCA], [http://pdbe.org/2zgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zgz RCSB], [http://www.ebi.ac.uk/pdbsum/2zgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zgz 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=2zgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zgz OCA], [https://pdbe.org/2zgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zgz RCSB], [https://www.ebi.ac.uk/pdbsum/2zgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zgz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PARM_ECOLX PARM_ECOLX]] Involved in the control of plasmid partition. Required for the accurate segregation of the plasmid. | + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fujisawa, T]] | + | [[Category: Fujisawa T]] |
| - | [[Category: Iwasa, M]] | + | [[Category: Iwasa M]] |
| - | [[Category: Maeda, K]] | + | [[Category: Maeda K]] |
| - | [[Category: Maeda, Y]] | + | [[Category: Maeda Y]] |
| - | [[Category: Matsuo, H]] | + | [[Category: Matsuo H]] |
| - | [[Category: Narita, A]] | + | [[Category: Narita A]] |
| - | [[Category: Nitanai, Y]] | + | [[Category: Nitanai Y]] |
| - | [[Category: Oda, T]] | + | [[Category: Oda T]] |
| - | [[Category: Onishi, H]] | + | [[Category: Onishi H]] |
| - | [[Category: Popp, D]] | + | [[Category: Popp D]] |
| - | [[Category: Parm]]
| + | |
| - | [[Category: Plasmid]]
| + | |
| - | [[Category: Plasmid partition]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
PARM_ECOLX Involved in the control of plasmid partition. Required for the accurate segregation of the plasmid.
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
ParM is a prokaryotic actin homologue, which ensures even plasmid segregation before bacterial cell division. In vivo, ParM forms a labile filament bundle that is reminiscent of the more complex spindle formed by microtubules partitioning chromosomes in eukaryotic cells. However, little is known about the underlying structural mechanism of DNA segregation by ParM filaments and the accompanying dynamic instability. Our biochemical, TIRF microscopy and high-pressure SAX observations indicate that polymerization and disintegration of ParM filaments is driven by GTP rather than ATP and that ParM acts as a GTP-driven molecular switch similar to a G protein. Image analysis of electron micrographs reveals that the ParM filament is a left-handed helix, opposed to the right-handed actin polymer. Nevertheless, the intersubunit contacts are similar to those of actin. Our atomic model of the ParM-GMPPNP filament, which also fits well to X-ray fibre diffraction patterns from oriented gels, can explain why after nucleotide release, large conformational changes of the protomer lead to a breakage of intra- and interstrand interactions, and thus to the observed disintegration of the ParM filament after DNA segregation.
Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability.,Popp D, Narita A, Oda T, Fujisawa T, Matsuo H, Nitanai Y, Iwasa M, Maeda K, Onishi H, Maeda Y EMBO J. 2008 Feb 6;27(3):570-9. Epub 2008 Jan 10. PMID:18188150[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Popp D, Narita A, Oda T, Fujisawa T, Matsuo H, Nitanai Y, Iwasa M, Maeda K, Onishi H, Maeda Y. Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability. EMBO J. 2008 Feb 6;27(3):570-9. Epub 2008 Jan 10. PMID:18188150
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