View source for 2bvu


==D83R mutant of Asaris suum major sperm protein (MSP)==
<StructureSection load='2bvu' size='340' side='right'caption='[[2bvu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bvu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BVU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=2bvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bvu OCA], [https://pdbe.org/2bvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bvu RCSB], [https://www.ebi.ac.uk/pdbsum/2bvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bvu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MSP1_ASCSU MSP1_ASCSU] Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/2bvu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2bvu ConSurf].
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== Publication Abstract from PubMed ==
Although several models have been proposed to account for how cytoskeleton polymerization drives protrusion in cell motility, the precise mechanism remains controversial. Here, we show that, in addition to force exerted directly against the membrane by growing filaments, the way elongating filaments pack also contributes to protrusion by generating an expansion of the cytoskeleton gel. Tomography shows that filament packing in the major sperm protein (MSP) -based nematode sperm-motility machinery resembles that observed with rigid rods. Maximum rod-packing density decreases dramatically as the rods lengthen. Therefore, as filaments elongate, the cytoskeleton gel expands to accommodate their packing less densely. This volume expansion combines with polymerization to drive protrusion. Consistent with this hypothesis, an engineered MSP mutant that generates shorter filaments shows higher filament-packing density and slower movement.

The role of filament-packing dynamics in powering amoeboid cell motility.,Miao L, Vanderlinde O, Liu J, Grant RP, Wouterse A, Shimabukuro K, Philipse A, Stewart M, Roberts TM Proc Natl Acad Sci U S A. 2008 Apr 8;105(14):5390-5. Epub 2008 Apr 2. PMID:18385381<ref>PMID:18385381</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2bvu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ascaris suum]]
[[Category: Large Structures]]
[[Category: Grant RP]]
[[Category: Roberts TM]]
[[Category: Stewart M]]