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==NMR solution structure of macro domain from Venezuelan equine encephalitis virus==
==NMR solution structure of macro domain from Venezuelan equine encephalitis virus==
<StructureSection load='5isn' size='340' side='right' caption='[[5isn]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
<StructureSection load='5isn' size='340' side='right'caption='[[5isn]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5isn]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISN FirstGlance]. <br>
<table><tr><td colspan='2'>[[5isn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eevvp Eevvp]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISN FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gqe|3gqe]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gqe|3gqe]]</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=5isn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isn OCA], [http://pdbe.org/5isn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isn RCSB], [http://www.ebi.ac.uk/pdbsum/5isn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isn ProSAT]</span></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=5isn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isn OCA], [http://pdbe.org/5isn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isn RCSB], [http://www.ebi.ac.uk/pdbsum/5isn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isn ProSAT]</span></td></tr>
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<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Macro domains consist of 130-190 amino acid residues and appear to be highly conserved in all kingdoms of life. Intense research on this field has shown that macro domains bind ADP-ribose and other similar molecules, but their exact function still remains intangible. Macro domains are highly conserved in the Alphavirus genus and the Venezuelan equine encephalitis virus (VEEV) is a member of this genus that causes fatal encephalitis to equines and humans. In this study we report the high yield recombinant expression and preliminary solution NMR study of the macro domain of VEEV. An almost complete sequence-specific assignment of its (1)H, (15)N and (13)C resonances was obtained and its secondary structure predicted by TALOS+. The protein shows a unique mixed alpha/beta-fold.
Venezuelan equine encephalitis virus (VEEV) is a new world alphavirus which can be involved in several central nervous system disorders such as encephalitis and meningitis. The VEEV genome codes for 4 non-structural proteins (nsP), of which nsP3 contains a Macro domain. Macro domains (MD) can be found as stand-alone proteins or embedded within larger proteins in viruses, bacteria and eukaryotes. Their most common feature is the binding of ADP-ribose (ADPr), while several macro domains act as ribosylation writers, erasers or readers. Alphavirus MD erase ribosylation but their precise contribution in viral replication is still under investigation. NMR-driven titration experiments of ADPr in solution with the VEEV macro domain (in apo- and complex state) show that it adopts a suitable conformation for ADPr binding. Specific experiments indicate that the flexibility of the loops beta5-alpha3 and alpha3-beta6 is critical for formation of the complex and assists a wrapping mechanism for ADPr binding. Furthermore, along with this sequence of events, the VEEV MD undergoes a conformational exchange process between the apo state and a low-populated "dark" conformational state.


NMR study of non-structural proteins--part II: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Venezuelan equine encephalitis virus (VEEV).,Makrynitsa GI, Ntonti D, Marousis KD, Tsika AC, Lichiere J, Papageorgiou N, Coutard B, Bentrop D, Spyroulias GA Biomol NMR Assign. 2015 Oct;9(2):247-51. doi: 10.1007/s12104-014-9584-9. Epub, 2014 Oct 8. PMID:25291978<ref>PMID:25291978</ref>
Conformational plasticity of the VEEV macro domain is important for binding of ADP-ribose.,Makrynitsa GI, Ntonti D, Marousis KD, Birkou M, Matsoukas MT, Asami S, Bentrop D, Papageorgiou N, Canard B, Coutard B, Spyroulias GA J Struct Biol. 2019 Apr 1;206(1):119-127. doi: 10.1016/j.jsb.2019.02.008. Epub, 2019 Feb 27. PMID:30825649<ref>PMID:30825649</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Eevvp]]
[[Category: Large Structures]]
[[Category: Bentrop, D]]
[[Category: Bentrop, D]]
[[Category: Coutard, B]]
[[Category: Coutard, B]]
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