1msp

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[[Image:1msp.png|left|200px]]
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==MAJOR SPERM PROTEIN, ALPHA ISOFORM (RECOMBINANT), PH 4.6==
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<StructureSection load='1msp' size='340' side='right' caption='[[1msp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1msp]] is a 2 chain structure with 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=1MSP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MSP FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALPHA MSP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6253 Ascaris suum])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1msp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1msp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1msp RCSB], [http://www.ebi.ac.uk/pdbsum/1msp PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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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/1msp_consurf.spt"</scriptWhenChecked>
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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/chain_selection.php?pdb_ID=2ata 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 ==
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We have determined the structure of the Ascaris major sperm protein (MSP) to 2.5 A resolution using X-ray crystallography. The MSP polypeptide chain has an immunoglobulin-like fold based on a seven-stranded beta sandwich. In two strands, cis-proline residues impart distinctive kinks, and overall the structure most closely resembles that of the N-terminal domain of the bacterial chaperonin, PapD. In the C2 crystal form which we have solved here, two MSP chains are tightly associated in the asymmetric unit and are related by a non-crystallographic 2-fold rotation axis. This arrangement almost certainly represents the MSP dimer that is present in solution. Additionally, the arrangement of two MSP dimers at one of the crystallographic 2-fold axes in the 215 A unit cell suggests a possible mode for the assembly of MSP into the filaments which promote cell movement. This dimer-dimer association is based on a beta sheet extension mechanism between adjoining MSP monomers which resembles the interaction between PapD and its protein substrate.
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{{STRUCTURE_1msp| PDB=1msp | SCENE= }}
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2.5 A resolution crystal structure of the motile major sperm protein (MSP) of Ascaris suum.,Bullock TL, Roberts TM, Stewart M J Mol Biol. 1996 Oct 25;263(2):284-96. PMID:8913307<ref>PMID:8913307</ref>
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===MAJOR SPERM PROTEIN, ALPHA ISOFORM (RECOMBINANT), PH 4.6===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_8913307}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1msp]] is a 2 chain structure with 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=1MSP OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:008913307</ref><ref group="xtra">PMID:011734033</ref><references group="xtra"/>
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[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
[[Category: Bullock, T L.]]
[[Category: Bullock, T L.]]

Revision as of 16:23, 28 September 2014

MAJOR SPERM PROTEIN, ALPHA ISOFORM (RECOMBINANT), PH 4.6

1msp, resolution 2.50Å

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