2w4b: Difference between revisions
No edit summary |
No edit summary |
||
| (13 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Epstein-Barr virus alkaline nuclease D203S mutant== | ||
<StructureSection load='2w4b' size='340' side='right'caption='[[2w4b]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2w4b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_4_strain_B95-8 Human herpesvirus 4 strain B95-8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W4B FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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=2w4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w4b OCA], [https://pdbe.org/2w4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w4b RCSB], [https://www.ebi.ac.uk/pdbsum/2w4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w4b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AN_EBVB9 AN_EBVB9] Displays DNase activity required for viral genome processing in the nucleus. Plays a role in processing non linear or branched viral DNA intermediates and in capsid egress from the host nucleus. Exhibits endonuclease and exonuclease activities and accepts both double-stranded and single-stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'-> 3' direction and the products are 5'-monophosphate nucleosides. Also acts as a cytoplasmic RNA endonuclease that induces degradation of the majority of the cellular messenger RNAs during lytic infection. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and evasion from host immune response.<ref>PMID:19264771</ref> | |||
== 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/w4/2w4b_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/main_output.php?pdb_ID=2w4b ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Epstein-Barr virus, a double-stranded DNA (dsDNA) virus, is a major human pathogen from the herpesvirus family. The nuclease is one of the lytic cycle proteins required for successful viral replication. In addition to the previously described endonuclease and exonuclease activities on single-stranded DNA and dsDNA substrates, we observed an RNase activity for Epstein-Barr virus nuclease in the presence of Mn(2+), giving a possible explanation for its role in host mRNA degradation. Its crystal structure shows a catalytic core of the D-(D/E)XK nuclease superfamily closely related to the exonuclease from bacteriophage lambda with a bridge across the active-site canyon. This bridge may reduce endonuclease activity, ensure processivity or play a role in strand separation of dsDNA substrates. As the DNA strand that is subject to cleavage is likely to make a sharp turn in front of the bridge, endonuclease activity on single-stranded DNA stretches appears to be possible, explaining the cleavage of circular substrates. | |||
A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities.,Buisson M, Geoui T, Flot D, Tarbouriech N, Ressing ME, Wiertz EJ, Burmeister WP J Mol Biol. 2009 Aug 28;391(4):717-28. Epub 2009 Jun 16. PMID:19538972<ref>PMID:19538972</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2w4b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Exonuclease 3D structures|Exonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human herpesvirus 4 strain B95-8]] | |||
[[Category: Large Structures]] | |||
[[Category: Buisson M]] | |||
[[Category: Burmeister WP]] | |||
[[Category: Flot D]] | |||
[[Category: Geoui T]] | |||
[[Category: Tarbouriech N]] | |||
Latest revision as of 18:43, 13 December 2023
Epstein-Barr virus alkaline nuclease D203S mutantEpstein-Barr virus alkaline nuclease D203S mutant
Structural highlights
FunctionAN_EBVB9 Displays DNase activity required for viral genome processing in the nucleus. Plays a role in processing non linear or branched viral DNA intermediates and in capsid egress from the host nucleus. Exhibits endonuclease and exonuclease activities and accepts both double-stranded and single-stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'-> 3' direction and the products are 5'-monophosphate nucleosides. Also acts as a cytoplasmic RNA endonuclease that induces degradation of the majority of the cellular messenger RNAs during lytic infection. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and evasion from host immune response.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEpstein-Barr virus, a double-stranded DNA (dsDNA) virus, is a major human pathogen from the herpesvirus family. The nuclease is one of the lytic cycle proteins required for successful viral replication. In addition to the previously described endonuclease and exonuclease activities on single-stranded DNA and dsDNA substrates, we observed an RNase activity for Epstein-Barr virus nuclease in the presence of Mn(2+), giving a possible explanation for its role in host mRNA degradation. Its crystal structure shows a catalytic core of the D-(D/E)XK nuclease superfamily closely related to the exonuclease from bacteriophage lambda with a bridge across the active-site canyon. This bridge may reduce endonuclease activity, ensure processivity or play a role in strand separation of dsDNA substrates. As the DNA strand that is subject to cleavage is likely to make a sharp turn in front of the bridge, endonuclease activity on single-stranded DNA stretches appears to be possible, explaining the cleavage of circular substrates. A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities.,Buisson M, Geoui T, Flot D, Tarbouriech N, Ressing ME, Wiertz EJ, Burmeister WP J Mol Biol. 2009 Aug 28;391(4):717-28. Epub 2009 Jun 16. PMID:19538972[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||