2msp

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[[Image:2msp.gif|left|200px]]
 
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{{Structure
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==MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5==
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|PDB= 2msp |SIZE=350|CAPTION= <scene name='initialview01'>2msp</scene>, resolution 3.3&Aring;
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<StructureSection load='2msp' size='340' side='right'caption='[[2msp]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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|GENE= BETA MSP C59S/T90C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6253 Ascaris suum])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2msp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msp OCA], [http://www.ebi.ac.uk/pdbsum/2msp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2msp RCSB]</span>
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[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.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/2msp_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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>
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2MSP is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9501910 9501910]
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</div>
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<div class="pdbe-citations 2msp" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bullock, T L.]]
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[[Category: Bullock TL]]
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[[Category: Mccoy, A J.]]
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[[Category: Mccoy AJ]]
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[[Category: Stewart, M.]]
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[[Category: Stewart M]]
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[[Category: cytoskeletal protein]]
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[[Category: filamentous protein structure]]
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[[Category: nematode sperm cell motility protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:04:25 2008''
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Current revision

MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5

PDB ID 2msp

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