7e1g
From Proteopedia
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==Structure of MreB3 from Spiroplasma eriocheiris== | ==Structure of MreB3 from Spiroplasma eriocheiris== | ||
| - | <StructureSection load='7e1g' size='340' side='right'caption='[[7e1g]]' scene=''> | + | <StructureSection load='7e1g' size='340' side='right'caption='[[7e1g]], [[Resolution|resolution]] 1.75Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E1G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7e1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Spiroplasma_eriocheiris Spiroplasma eriocheiris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E1G FirstGlance]. <br> |
| - | </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=7e1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e1g OCA], [https://pdbe.org/7e1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e1g RCSB], [https://www.ebi.ac.uk/pdbsum/7e1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e1g ProSAT]</span></td></tr> | + | </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>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</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=7e1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e1g OCA], [https://pdbe.org/7e1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e1g RCSB], [https://www.ebi.ac.uk/pdbsum/7e1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e1g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0H3XJK5_9MOLU A0A0H3XJK5_9MOLU] Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature.[HAMAP-Rule:MF_02207] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | MreB is a bacterial protein belonging to the actin superfamily. This protein polymerizes into an antiparallel double-stranded filament that determines cell shape by maintaining cell wall synthesis. Spiroplasma eriocheiris, a helical wall-less bacterium, has five MreB homologous (SpeMreB1-5) that probably contribute to swimming motility. Here, we investigated the structure, ATPase activity and polymerization dynamics of SpeMreB3 and SpeMreB5. SpeMreB3 polymerized into a double-stranded filament with possible antiparallel polarity, while SpeMreB5 formed sheets which contained the antiparallel filament, upon nucleotide binding. SpeMreB3 showed slow P(i) release owing to the lack of an amino acid motif conserved in the catalytic centre of MreB family proteins. Our SpeMreB3 crystal structures and analyses of SpeMreB3 and SpeMreB5 variants showed that the amino acid motif probably plays a role in eliminating a nucleophilic water proton during ATP hydrolysis. Sedimentation assays suggest that SpeMreB3 has a lower polymerization activity than SpeMreB5, though their polymerization dynamics are qualitatively similar to those of other actin superfamily proteins, in which pre-ATP hydrolysis and post-P(i) release states are unfavourable for them to remain as filaments. | ||
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| + | ATP-dependent polymerization dynamics of bacterial actin proteins involved in Spiroplasma swimming.,Takahashi D, Fujiwara I, Sasajima Y, Narita A, Imada K, Miyata M Open Biol. 2022 Oct;12(10):220083. doi: 10.1098/rsob.220083. Epub 2022 Oct 26. PMID:36285441<ref>PMID:36285441</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7e1g" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Spiroplasma eriocheiris]] | ||
[[Category: Imada K]] | [[Category: Imada K]] | ||
[[Category: Miyata M]] | [[Category: Miyata M]] | ||
[[Category: Takahashi D]] | [[Category: Takahashi D]] | ||
Revision as of 07:41, 8 March 2023
Structure of MreB3 from Spiroplasma eriocheiris
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