5y2h
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the oligomerization domain of NSP4 from the rotavirus strain MF66== | |
| + | <StructureSection load='5y2h' size='340' side='right' caption='[[5y2h]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5y2h]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y2H FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5y2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y2h OCA], [http://pdbe.org/5y2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y2h RCSB], [http://www.ebi.ac.uk/pdbsum/5y2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y2h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rotavirus nonstructural protein 4, the first viral enterotoxin to be identified, is a multidomain, multifunctional glycoprotein. Earlier, we reported a Ca(2+)-bound coiled-coil tetrameric structure of the diarrhea-inducing region of NSP4 from the rotavirus strains SA11 and I321 and a Ca(2+)-free pentameric structure from the rotavirus strain ST3, all with a parallel arrangement of alpha-helices. pH was found to determine the oligomeric state: a basic pH favoured a tetramer, whereas an acidic pH favoured a pentamer. Here, we report two novel forms of the coiled-coil region of NSP4 from the bovine rotavirus strains MF66 and NCDV. These crystallized at acidic pH, forming antiparallel coiled-coil tetrameric structures without any bound Ca(2+) ion. Structural and mutational studies of the coiled-coil regions of NSP4 revealed that the nature of the residue at position 131 (Tyr/His) plays an important role in the observed structural diversity. | ||
| - | + | New tetrameric forms of the rotavirus NSP4 with antiparallel helices.,Kumar S, Ramappa R, Pamidimukkala K, Rao CD, Suguna K Arch Virol. 2018 Feb 17. pii: 10.1007/s00705-018-3753-6. doi:, 10.1007/s00705-018-3753-6. PMID:29455326<ref>PMID:29455326</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5y2h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kumar, S]] | ||
| + | [[Category: Suguna, K]] | ||
| + | [[Category: Antiparallel tetramer nsp4 rotavirus coiled-coil mf66]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 06:26, 14 March 2018
Crystal structure of the oligomerization domain of NSP4 from the rotavirus strain MF66
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