2o1j: Difference between revisions
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<StructureSection load='2o1j' size='340' side='right'caption='[[2o1j]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2o1j' size='340' side='right'caption='[[2o1j]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2o1j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rotavirus_str. | <table><tr><td colspan='2'>[[2o1j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rotavirus_str._I321 Rotavirus str. I321]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O1J FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1j OCA], [https://pdbe.org/2o1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1j RCSB], [https://www.ebi.ac.uk/pdbsum/2o1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1j ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1j OCA], [https://pdbe.org/2o1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1j RCSB], [https://www.ebi.ac.uk/pdbsum/2o1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9PYC1_9VIRU Q9PYC1_9VIRU] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o1j ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o1j ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rotavirus nonstructural protein 4 (NSP4) is a multidomainal and multifunctional protein and is recognized as the first virus-encoded enterotoxin. Extensive efforts to crystallize the complete cytoplasmic tail (CT), which exhibits all the known biological functions, have been unsuccessful, and to date, the structure of only a synthetic peptide corresponding to amino acids (aa) 95-137 has been reported. Recent studies indicate that the interspecies-variable domain (ISVD) from aa 135 to 141 as well as the extreme C-terminus are critical determinants of virus virulence and the diarrhea-inducing ability of the protein. Among the five NSP4 genotypes identified, those belonging to genotypes A1, B and C possess either a proline at position 138 or a glycine at 140, while those of A2, D and E lack these residues in the ISVD, suggesting conformational differences in this region among different NSP4s. Here, we examined the crystallization properties of several deletion mutants and report the structure of a recombinant mutant, NSP4:95-146, lacking the N-terminal 94 and C-terminal 29 aa, from SA11 (A1) and I321 (A2) at 1.67 and 2.7 A, respectively. In spite of the high resolution of one of the structures, electron density for the C-terminal 9 residues could not be seen for either of the mutants, and the crystal packing resulted in the creation of a clear empty space for this region. Extension of the unstructured C-terminus beyond aa 146 hindered crystallization under the experimental conditions. The present structure revealed significant differences from that of the synthetic peptide in the conformation of amino acids at the end of the helix as well as the crystal packing owing to the additional space required to accommodate the un structured virulence-determining region. The crystal structure and secondary structure prediction of the NSP4:95-146 mutants from different genotypes suggest that the region C-terminal to aa 137 in all the NSP4 proteins is likely to be unstructured, and this might be of structural and biological functional significance. | |||
Structure of the extended diarrhea-inducing domain of rotavirus enterotoxigenic protein NSP4.,Deepa R, Durga Rao C, Suguna K Arch Virol. 2007;152(5):847-59. doi: 10.1007/s00705-006-0921-x. Epub 2007 Jan 31. PMID:17265103<ref>PMID:17265103</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2o1j" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]] | *[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rotavirus str. | [[Category: Rotavirus str. I321]] | ||
[[Category: Deepa | [[Category: Deepa R]] | ||
[[Category: Rao | [[Category: Durga Rao C]] | ||
[[Category: Suguna | [[Category: Suguna K]] | ||
Revision as of 03:13, 28 December 2023
Structure of the extended diarrhea-inducing domain of rotavirus enterotoxigenic protein NSP4Structure of the extended diarrhea-inducing domain of rotavirus enterotoxigenic protein NSP4
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRotavirus nonstructural protein 4 (NSP4) is a multidomainal and multifunctional protein and is recognized as the first virus-encoded enterotoxin. Extensive efforts to crystallize the complete cytoplasmic tail (CT), which exhibits all the known biological functions, have been unsuccessful, and to date, the structure of only a synthetic peptide corresponding to amino acids (aa) 95-137 has been reported. Recent studies indicate that the interspecies-variable domain (ISVD) from aa 135 to 141 as well as the extreme C-terminus are critical determinants of virus virulence and the diarrhea-inducing ability of the protein. Among the five NSP4 genotypes identified, those belonging to genotypes A1, B and C possess either a proline at position 138 or a glycine at 140, while those of A2, D and E lack these residues in the ISVD, suggesting conformational differences in this region among different NSP4s. Here, we examined the crystallization properties of several deletion mutants and report the structure of a recombinant mutant, NSP4:95-146, lacking the N-terminal 94 and C-terminal 29 aa, from SA11 (A1) and I321 (A2) at 1.67 and 2.7 A, respectively. In spite of the high resolution of one of the structures, electron density for the C-terminal 9 residues could not be seen for either of the mutants, and the crystal packing resulted in the creation of a clear empty space for this region. Extension of the unstructured C-terminus beyond aa 146 hindered crystallization under the experimental conditions. The present structure revealed significant differences from that of the synthetic peptide in the conformation of amino acids at the end of the helix as well as the crystal packing owing to the additional space required to accommodate the un structured virulence-determining region. The crystal structure and secondary structure prediction of the NSP4:95-146 mutants from different genotypes suggest that the region C-terminal to aa 137 in all the NSP4 proteins is likely to be unstructured, and this might be of structural and biological functional significance. Structure of the extended diarrhea-inducing domain of rotavirus enterotoxigenic protein NSP4.,Deepa R, Durga Rao C, Suguna K Arch Virol. 2007;152(5):847-59. doi: 10.1007/s00705-006-0921-x. Epub 2007 Jan 31. PMID:17265103[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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