2msp
From Proteopedia
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[[Image:2msp.gif|left|200px]] | [[Image:2msp.gif|left|200px]] | ||
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'''MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5''' | '''MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5''' | ||
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[[Category: Mccoy, A J.]] | [[Category: Mccoy, A J.]] | ||
[[Category: Stewart, M.]] | [[Category: Stewart, M.]] | ||
| - | [[Category: | + | [[Category: Cytoskeletal protein]] |
| - | [[Category: | + | [[Category: Filamentous protein structure]] |
| - | [[Category: | + | [[Category: Nematode sperm cell motility protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:34:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:34, 4 May 2008
MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5
Overview
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.
About this Structure
2MSP is a Single protein structure of sequence from Ascaris suum. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 09:34:46 2008
