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| | <StructureSection load='2bjr' size='340' side='right'caption='[[2bjr]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2bjr' size='340' side='right'caption='[[2bjr]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bjr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascsu Ascsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BJR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bjr]] is a 2 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=2BJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BJR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bjq|2bjq]]</div></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=2bjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjr OCA], [https://pdbe.org/2bjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bjr RCSB], [https://www.ebi.ac.uk/pdbsum/2bjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjr 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=2bjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjr OCA], [https://pdbe.org/2bjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bjr RCSB], [https://www.ebi.ac.uk/pdbsum/2bjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7YXJ9_ASCSU Q7YXJ9_ASCSU] |
| | == 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: Ascsu]] | + | [[Category: Ascaris suum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buttery, S M]] | + | [[Category: Buttery SM]] |
| - | [[Category: Ekman, G C]] | + | [[Category: Ekman GC]] |
| - | [[Category: Grant, R P]] | + | [[Category: Grant RP]] |
| - | [[Category: Roberts, T M]] | + | [[Category: Roberts TM]] |
| - | [[Category: Stewart, M]] | + | [[Category: Stewart M]] |
| - | [[Category: Ascari]]
| + | |
| - | [[Category: Motility]]
| + | |
| - | [[Category: Msp]]
| + | |
| - | [[Category: Nematode]]
| + | |
| Structural highlights
Function
Q7YXJ9_ASCSU
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
The simplicity and specialization of the cell motility machinery of Ascaris sperm provides a powerful system in which to probe the basic molecular mechanism of amoeboid cell motility. Although Ascaris sperm locomotion closely resembles that seen in many other types of crawling cell, movement is generated by modulation of a cytoskeleton based on the major sperm protein (MSP) rather than the actin present in other cell types. The Ascaris motility machinery can be studied conveniently in a cell-free in vitro system based on the movement of plasma membrane vesicles by fibres constructed from bundles of MSP filaments. In addition to ATP, MSP and a plasma membrane protein, reconstitution of MSP motility in this cell-free extract requires cytosolic proteins to orchestrate the site-specific assembly and bundling of MSP filaments that generates locomotion. One of these proteins, MFP2, accelerates the rate of movement in this assay. Here, we describe crystal structures of two isoforms of MFP2 and show that both are constructed from two domains that have the same fold based on a novel, compact beta sheet arrangement. Patterns of conservation observed in a structure-based analysis of MFP2 sequences from different nematode species identified regions that may be putative functional interfaces involved both in interactions between MFP2 domains and also with other components of the sperm motility machinery. Analysis of the growth of fibres in vitro in the presence of added MFP2 indicated that MFP2 increases the rate of locomotion by enhancing the effective rate of MSP filament polymerization. This observation, together with the structural data, suggests that MFP2 may function in a manner analogous to formins in actin-based motility.
Structure of MFP2 and its function in enhancing MSP polymerization in Ascaris sperm amoeboid motility.,Grant RP, Buttery SM, Ekman GC, Roberts TM, Stewart M J Mol Biol. 2005 Apr 1;347(3):583-95. PMID:15755452[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grant RP, Buttery SM, Ekman GC, Roberts TM, Stewart M. Structure of MFP2 and its function in enhancing MSP polymerization in Ascaris sperm amoeboid motility. J Mol Biol. 2005 Apr 1;347(3):583-95. PMID:15755452 doi:http://dx.doi.org/10.1016/j.jmb.2005.01.054
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