1g1i
From Proteopedia
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| - | [[Image:1g1i.gif|left|200px]] | + | [[Image:1g1i.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4''' | + | {{Structure |
| + | |PDB= 1g1i |SIZE=350|CAPTION= <scene name='initialview01'>1g1i</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G1I is a [ | + | 1G1I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1I 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/11124032 11124032] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bowman, G D.]] | [[Category: Bowman, G D.]] | ||
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[[Category: parallel coiled-coil]] | [[Category: parallel coiled-coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:53 2008'' |
Revision as of 09:16, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1G1I is a Single protein structure of sequence from [1]. 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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