1msp

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(New page: 200px<br /><applet load="1msp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1msp, resolution 2.5&Aring;" /> '''MAJOR SPERM PROTEIN, ...)
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[[Image:1msp.gif|left|200px]]<br /><applet load="1msp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1msp, resolution 2.5&Aring;" />
caption="1msp, resolution 2.5&Aring;" />
'''MAJOR SPERM PROTEIN, ALPHA ISOFORM (RECOMBINANT), PH 4.6'''<br />
'''MAJOR SPERM PROTEIN, ALPHA ISOFORM (RECOMBINANT), PH 4.6'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1MSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MSP OCA].
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1MSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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].
==Reference==
==Reference==
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[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bullock, T.L.]]
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[[Category: Bullock, T L.]]
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[[Category: Roberts, T.M.]]
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[[Category: Roberts, T M.]]
[[Category: Stewart, M.]]
[[Category: Stewart, M.]]
[[Category: cell motility protein]]
[[Category: cell motility protein]]
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[[Category: sperm]]
[[Category: sperm]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:40:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:39 2008''

Revision as of 11:58, 21 February 2008


1msp, resolution 2.5Å

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

Overview

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.

About this Structure

1MSP is a Single protein structure of sequence from Ascaris suum. Full crystallographic information is available from OCA.

Reference

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

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