2MSP

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

Summary for 2MSP

• Entry DOI: 10.2210/pdb2msp/pdb
• Descriptor: MAJOR SPERM PROTEIN (1 entity in total)
• Functional Keywords: cytoskeletal protein, nematode sperm cell motility protein, filamentous protein structure, cell motility protein
• Biological source: Ascaris suum (pig roundworm)
• Cellular location: Cell projection, pseudopodium: P27440
• Total number of polymer chains: 8
• Total formula weight: 112967.01

Authors

Bullock, T.L.,Mccoy, A.J.,Stewart, M. (deposition date: 1997-12-19, release date: 1998-04-15, Last modification date: 2024-05-22)

Primary citation

Bullock, T.L.,McCoy, A.J.,Kent, H.M.,Roberts, T.M.,Stewart, M.
Structural basis for amoeboid motility in nematode sperm.
Nat.Struct.Biol., 5:184-189, 1998

PubMed Abstract: 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.

PubMed: 9501910
DOI: 10.1038/nsb0398-184

Experimental method

X-RAY DIFFRACTION (3.3 Å)