6iug: Difference between revisions

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<SX load='6iug' size='340' side='right' viewer='molstar' caption='[[6iug]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
<SX load='6iug' size='340' side='right' viewer='molstar' caption='[[6iug]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6iug]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IUG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6IUG FirstGlance]. <br>
<table><tr><td colspan='2'>[[6iug]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IUG 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">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</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=6iug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iug OCA], [http://pdbe.org/6iug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iug RCSB], [http://www.ebi.ac.uk/pdbsum/6iug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iug ProSAT]</span></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=6iug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iug OCA], [https://pdbe.org/6iug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iug RCSB], [https://www.ebi.ac.uk/pdbsum/6iug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iug ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/B6TQ08_MAIZE B6TQ08_MAIZE]
Actins are among the most abundant and conserved proteins in plant, mammalian and other eukaryotic cells, where they form filamentous structures to perform vital roles in key cellular processes. Although large amounts of data on the biochemical activities, dynamic behaviors and important cellular functions of plant actin filaments have been accumulated, their structural basis is still elusive. Here, we report a 3.9 A structure of the plant actin filament (ZMPA) from Zea mays pollen using cryo-electron microscopy. The structure shows a right-handed, parallel and staggered architecture that is stabilized by intra- and interstrand interactions. While the overall structure resembles that of other actin filaments, its DNase I-binding loop (D-loop) bends further outward, adopting an open conformation similar to that of the jasplakinolide- or BeFx-stabil1ized rabbit skeleton muscle actin (RSMA) filament. Single-molecule magnetic tweezers analysis revealed that the ZMPA filament can resist greater stretching force than the RSMA filament. Overall, these data provide evidence that plant actin filaments have greater stability than animal actin filaments, which is important for their roles as tracks for long-distance vesicle and organelle transportation.


Cryo-EM Structure of Actin Filaments from Zea mays Pollen.,Ren Z, Zhang Y, Zhang Y, He Y, Du P, Wang Z, Sun F, Ren H Plant Cell. 2019 Oct 18. pii: tpc.18.00973. doi: 10.1105/tpc.18.00973. PMID:31628168<ref>PMID:31628168</ref>
==See Also==
 
*[[Actin 3D structures|Actin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iug" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Du, P Z]]
[[Category: Du PZ]]
[[Category: He, Y Q]]
[[Category: He YQ]]
[[Category: Ren, H Y]]
[[Category: Ren HY]]
[[Category: Ren, Z H]]
[[Category: Ren ZH]]
[[Category: Sun, F]]
[[Category: Sun F]]
[[Category: Wang, Z X]]
[[Category: Wang ZX]]
[[Category: Zhang, Y]]
[[Category: Zhang Y]]
[[Category: Actin]]
[[Category: Helix]]
[[Category: Microfilament]]
[[Category: Protein fibril]]

Latest revision as of 10:35, 27 March 2024

Cryo-EM structure of the plant actin filaments from Zea mays pollen

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