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2bjq

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{{STRUCTURE_2bjq| PDB=2bjq | SCENE= }}
{{STRUCTURE_2bjq| PDB=2bjq | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE NEMATODE SPERM CELL MOTILITY PROTEIN MFP2'''
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===CRYSTAL STRUCTURE OF THE NEMATODE SPERM CELL MOTILITY PROTEIN MFP2===
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==Overview==
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The simplicity and specialization of the cell motility machinery of Ascaris sperm provides a powerful system in which to probe the basic molecular mechanism of amoeboid cell motility. Although Ascaris sperm locomotion closely resembles that seen in many other types of crawling cell, movement is generated by modulation of a cytoskeleton based on the major sperm protein (MSP) rather than the actin present in other cell types. The Ascaris motility machinery can be studied conveniently in a cell-free in vitro system based on the movement of plasma membrane vesicles by fibres constructed from bundles of MSP filaments. In addition to ATP, MSP and a plasma membrane protein, reconstitution of MSP motility in this cell-free extract requires cytosolic proteins to orchestrate the site-specific assembly and bundling of MSP filaments that generates locomotion. One of these proteins, MFP2, accelerates the rate of movement in this assay. Here, we describe crystal structures of two isoforms of MFP2 and show that both are constructed from two domains that have the same fold based on a novel, compact beta sheet arrangement. Patterns of conservation observed in a structure-based analysis of MFP2 sequences from different nematode species identified regions that may be putative functional interfaces involved both in interactions between MFP2 domains and also with other components of the sperm motility machinery. Analysis of the growth of fibres in vitro in the presence of added MFP2 indicated that MFP2 increases the rate of locomotion by enhancing the effective rate of MSP filament polymerization. This observation, together with the structural data, suggests that MFP2 may function in a manner analogous to formins in actin-based motility.
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{{ABSTRACT_PUBMED_15755452}}
==About this Structure==
==About this Structure==
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[[Category: Msp]]
[[Category: Msp]]
[[Category: Nematode]]
[[Category: Nematode]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:39:19 2008''

Revision as of 10:39, 28 July 2008

Image:2bjq.png

Template:STRUCTURE 2bjq

CRYSTAL STRUCTURE OF THE NEMATODE SPERM CELL MOTILITY PROTEIN MFP2

Template:ABSTRACT PUBMED 15755452

About this Structure

2BJQ is a Single protein structure of sequence from Ascaris suum. Full crystallographic information is available from OCA.

Reference

Structure of MFP2 and its function in enhancing MSP polymerization in Ascaris sperm amoeboid motility., Grant RP, Buttery SM, Ekman GC, Roberts TM, Stewart M, J Mol Biol. 2005 Apr 1;347(3):583-95. PMID:15755452

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