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New page: left|200px<br /><applet load="1g1j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g1j, resolution 1.86Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1g1j.gif|left|200px]]<br /><applet load="1g1j" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1g1j.gif|left|200px]]<br /><applet load="1g1j" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g1j, resolution 1.86&Aring;" />
caption="1g1j, resolution 1.86&Aring;" />
'''CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4'''<br />
'''CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4'''<br />


==Overview==
==Overview==
During the maturation of rotaviral particles, non-structural protein 4, (NSP4) plays a critical role in the translocation of the immature capsid, into the lumen of the endoplasmic reticulum. Full-length NSP4 and a 22, amino acid peptide (NSP4(114-135)) derived from this protein have been, shown to induce diarrhea in young mice in an age-dependent manner, and may, therefore be the agent responsible for rotavirally-induced symptoms. We, have determined the crystal structure of the oligomerization domain of, NSP4 which spans residues 95 to 137 (NSP4(95-137)). NSP4(95-137), self-associates into a parallel, tetrameric coiled-coil, with the, hydrophobic core interrupted by three polar layers occupying a and, d-heptad positions. Side-chains from two consecutive polar layers, consisting of four Gln123 and two of the four Glu120 residues, coordinate, a divalent cation. Two independent structures built from MAD-phased data, indicated the presence of a strontium and calcium ion bound at this site, respectively. This metal-binding site appears to play an important role in, stabilizing the homo-tetramer, which has implications for the engagement, of NSP4 as an enterotoxin.
During the maturation of rotaviral particles, non-structural protein 4 (NSP4) plays a critical role in the translocation of the immature capsid into the lumen of the endoplasmic reticulum. Full-length NSP4 and a 22 amino acid peptide (NSP4(114-135)) derived from this protein have been shown to induce diarrhea in young mice in an age-dependent manner, and may therefore be the agent responsible for rotavirally-induced symptoms. We have determined the crystal structure of the oligomerization domain of NSP4 which spans residues 95 to 137 (NSP4(95-137)). NSP4(95-137) self-associates into a parallel, tetrameric coiled-coil, with the hydrophobic core interrupted by three polar layers occupying a and d-heptad positions. Side-chains from two consecutive polar layers, consisting of four Gln123 and two of the four Glu120 residues, coordinate a divalent cation. Two independent structures built from MAD-phased data indicated the presence of a strontium and calcium ion bound at this site, respectively. This metal-binding site appears to play an important role in stabilizing the homo-tetramer, which has implications for the engagement of NSP4 as an enterotoxin.


==About this Structure==
==About this Structure==
1G1J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G1J OCA].  
1G1J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SR:'>SR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1J OCA].  


==Reference==
==Reference==
Crystal structure of the oligomerization domain of NSP4 from rotavirus reveals a core metal-binding site., Bowman GD, Nodelman IM, Levy O, Lin SL, Tian P, Zamb TJ, Udem SA, Venkataraghavan B, Schutt CE, J Mol Biol. 2000 Dec 15;304(5):861-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11124032 11124032]
Crystal structure of the oligomerization domain of NSP4 from rotavirus reveals a core metal-binding site., Bowman GD, Nodelman IM, Levy O, Lin SL, Tian P, Zamb TJ, Udem SA, Venkataraghavan B, Schutt CE, J Mol Biol. 2000 Dec 15;304(5):861-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11124032 11124032]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bowman, G.D.]]
[[Category: Bowman, G D.]]
[[Category: Nodelman, I.M.]]
[[Category: Nodelman, I M.]]
[[Category: Schutt, C.E.]]
[[Category: Schutt, C E.]]
[[Category: SR]]
[[Category: SR]]
[[Category: cation]]
[[Category: cation]]
Line 23: Line 23:
[[Category: strontium]]
[[Category: strontium]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:37:24 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:00 2008''

Revision as of 10:45, 21 February 2008

File:1g1j.gif


1g1j, resolution 1.86Å

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CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4

Overview

During the maturation of rotaviral particles, non-structural protein 4 (NSP4) plays a critical role in the translocation of the immature capsid into the lumen of the endoplasmic reticulum. Full-length NSP4 and a 22 amino acid peptide (NSP4(114-135)) derived from this protein have been shown to induce diarrhea in young mice in an age-dependent manner, and may therefore be the agent responsible for rotavirally-induced symptoms. We have determined the crystal structure of the oligomerization domain of NSP4 which spans residues 95 to 137 (NSP4(95-137)). NSP4(95-137) self-associates into a parallel, tetrameric coiled-coil, with the hydrophobic core interrupted by three polar layers occupying a and d-heptad positions. Side-chains from two consecutive polar layers, consisting of four Gln123 and two of the four Glu120 residues, coordinate a divalent cation. Two independent structures built from MAD-phased data indicated the presence of a strontium and calcium ion bound at this site, respectively. This metal-binding site appears to play an important role in stabilizing the homo-tetramer, which has implications for the engagement of NSP4 as an enterotoxin.

About this Structure

1G1J is a Single protein structure of sequence from [1] with SR as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the oligomerization domain of NSP4 from rotavirus reveals a core metal-binding site., Bowman GD, Nodelman IM, Levy O, Lin SL, Tian P, Zamb TJ, Udem SA, Venkataraghavan B, Schutt CE, J Mol Biol. 2000 Dec 15;304(5):861-71. PMID:11124032

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