2msp
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2msp.png|left|200px]] | ||
- | < | + | ==MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5== |
- | + | <StructureSection load='2msp' size='340' side='right'caption='[[2msp]], [[Resolution|resolution]] 3.30Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2msp]] is a 8 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=2MSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSP 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]] 3.3Å</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=2msp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msp OCA], [https://pdbe.org/2msp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msp RCSB], [https://www.ebi.ac.uk/pdbsum/2msp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msp ProSAT]</span></td></tr> | |
- | + | </table> | |
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/MSP2_ASCSU MSP2_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/ms/2msp_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=2msp ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Cell locomotion in amoeboid nematode sperm is generated by the vectorial assembly and bundling of filaments of the major sperm protein (MSP). MSP filaments are constructed from two helical subfilaments and here we describe the structure of putative MSP subfilament helices determined by X-ray crystallography at 3.3 A resolution. In addition to establishing the interfaces involved in polymerization, this structural model shows that the MSP helices are constructed from dimers and have no overall polarity, suggesting that it is unlikely that molecular motors play a direct role in the generation of protrusive force in these amoeboid cells. | ||
- | + | Structural basis for amoeboid motility in nematode sperm.,Bullock TL, McCoy AJ, Kent HM, Roberts TM, Stewart M Nat Struct Biol. 1998 Mar;5(3):184-9. PMID:9501910<ref>PMID:9501910</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2msp" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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- | == | + | |
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[[Category: Ascaris suum]] | [[Category: Ascaris suum]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Bullock | + | [[Category: Bullock TL]] |
- | [[Category: Mccoy | + | [[Category: Mccoy AJ]] |
- | [[Category: Stewart | + | [[Category: Stewart M]] |
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Current revision
MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5
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