View source for 4apw


==Alp12 filament structure==
<SX load='4apw' size='340' side='right' viewer='molstar' caption='[[4apw]], [[Resolution|resolution]] 19.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4apw]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4APW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4APW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 19.7&#8491;</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=4apw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apw OCA], [https://pdbe.org/4apw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4apw RCSB], [https://www.ebi.ac.uk/pdbsum/4apw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4apw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q89A01_CLOTE Q89A01_CLOTE] 
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== Publication Abstract from PubMed ==
Eukaryotic F-actin is constructed from two protofilaments that gently wind around each other to form a helical polymer. Several bacterial actin-like proteins (Alps) are also known to form F-actin-like helical arrangements from two protofilaments, yet with varied helical geometries. Here, we report a unique filament architecture of Alp12 from Clostridium tetani that is constructed from four protofilaments. Through fitting of an Alp12 monomer homology model into the electron microscopy data, the filament was determined to be constructed from two antiparallel strands, each composed of two parallel protofilaments. These four protofilaments form an open helical cylinder separated by a wide cleft. The molecular interactions within single protofilaments are similar to F-actin, yet interactions between protofilaments differ from those in F-actin. The filament structure and assembly and disassembly kinetics suggest Alp12 to be a dynamically unstable force-generating motor involved in segregating the pE88 plasmid, which encodes the lethal tetanus toxin, and thus a potential target for drug design. Alp12 can be repeatedly cycled between states of polymerization and dissociation, making it a novel candidate for incorporation into fuel-propelled nanobiopolymer machines.

Novel Actin-like Filament Structure from Clostridium tetani.,Popp D, Narita A, Lee LJ, Ghoshdastider U, Xue B, Srinivasan R, Balasubramanian MK, Tanaka T, Robinson RC J Biol Chem. 2012 Jun 15;287(25):21121-9. Epub 2012 Apr 18. PMID:22514279<ref>PMID:22514279</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4apw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</SX>
[[Category: Clostridium tetani]]
[[Category: Large Structures]]
[[Category: Balasubramanian MK]]
[[Category: Ghoshdastider U]]
[[Category: Lee LJ]]
[[Category: Narita A]]
[[Category: Popp D]]
[[Category: Robinson RC]]
[[Category: Srinivasan R]]
[[Category: Tanaka T]]
[[Category: Xue B]]