2jzf
From Proteopedia
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- | [[ | + | ==NMR Conformer closest to the mean coordinates of the domain 513-651 of the SARS-CoV nonstructural protein nsp3== |
+ | <StructureSection load='2jzf' size='340' side='right' caption='[[2jzf]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2jzf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jwj 2jwj]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JZF FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rnk|2rnk]], [[2jzd|2jzd]], [[2jze|2jze]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rep, 1a-1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 SARS coronavirus])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jzf RCSB], [http://www.ebi.ac.uk/pdbsum/2jzf PDBsum], [http://www.topsan.org/Proteins/JCSG/2jzf TOPSAN]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jzf_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for "middle of the SARS-unique domain") in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection. | ||
- | + | Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.,Chatterjee A, Johnson MA, Serrano P, Pedrini B, Joseph JS, Neuman BW, Saikatendu K, Buchmeier MJ, Kuhn P, Wuthrich K J Virol. 2009 Feb;83(4):1823-36. Epub 2008 Dec 3. PMID:19052085<ref>PMID:19052085</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Nonstructural protein|Nonstructural protein]] | *[[Nonstructural protein|Nonstructural protein]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus]] | ||
[[Category: Buchmeier, M J.]] | [[Category: Buchmeier, M J.]] |
Revision as of 02:29, 29 September 2014
NMR Conformer closest to the mean coordinates of the domain 513-651 of the SARS-CoV nonstructural protein nsp3
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Categories: Sars coronavirus | Buchmeier, M J. | Chatterjee, A. | JCSG, Joint Center for Structural Genomics. | Johnson, M A. | Joseph, J. | Kuhn, P. | Neuman, B. | Pedrini, B. | Saikatendu, K. | Serrano, P. | Stevens, R C. | Wilson, I A. | Wuthrich, K. | Functional and structural proteomics of sars-cov- related protein | Jcsg | Joint center for structural genomic | Nonstructural protein | Nsp3 | Nsp3c | Protein structure initiative | Psi-2 | Sars-cov | Sars-unique domain | Structural genomic | Viral protein