2msp

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

spinqualitylabelsall models 2msp, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2msp is a 8 chain structure with sequence from Ascaris suum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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