1sh0: Difference between revisions
No edit summary |
No edit summary |
||
(7 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Crystal Structure of Norwalk Virus Polymerase (Triclinic)== | |||
<StructureSection load='1sh0' size='340' side='right'caption='[[1sh0]], [[Resolution|resolution]] 2.17Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1sh0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SH0 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]] 2.17Å</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=1sh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sh0 OCA], [https://pdbe.org/1sh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sh0 RCSB], [https://www.ebi.ac.uk/pdbsum/1sh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sh0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q70ET3_9CALI Q70ET3_9CALI] | |||
== 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/sh/1sh0_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=1sh0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Norwalk virus is a major cause of acute gastroenteritis for which effective treatments are sorely lacking. To provide a basis for the rational design of novel antiviral agents, the main replication enzyme in Norwalk virus, the virally encoded RNA-dependent RNA polymerase (RdRP), has been expressed in an enzymatically active form, and its structure has been crystallographically determined both in the presence and absence of divalent metal cations. Although the overall fold of the enzyme is similar to that seen previously in the RdRP from rabbit hemorrhagic disease virus, the carboxyl terminus, surprisingly, is located in the active site cleft in five independent copies of the protein in three distinct crystal forms. The location of this carboxyl-terminal segment appears to interfere with the binding of double-stranded RNA in the active site cleft and may play a role in the initiation of RNA synthesis or mediate interactions with accessory replication proteins. | |||
Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft.,Ng KK, Pendas-Franco N, Rojo J, Boga JA, Machin A, Alonso JM, Parra F J Biol Chem. 2004 Apr 16;279(16):16638-45. Epub 2004 Feb 5. PMID:14764591<ref>PMID:14764591</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1sh0" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[RNA polymerase|RNA polymerase]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Norwalk virus]] | [[Category: Norwalk virus]] | ||
[[Category: Alonso JM]] | |||
[[Category: Alonso | [[Category: Boga JA]] | ||
[[Category: Boga | [[Category: Machin A]] | ||
[[Category: Machin | [[Category: Ng KK]] | ||
[[Category: Ng | [[Category: Parra F]] | ||
[[Category: Parra | [[Category: Pendas-Franco N]] | ||
[[Category: Pendas-Franco | [[Category: Rojo J]] | ||
[[Category: Rojo | |||
Latest revision as of 09:16, 23 August 2023
Crystal Structure of Norwalk Virus Polymerase (Triclinic)Crystal Structure of Norwalk Virus Polymerase (Triclinic)
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 PubMedNorwalk virus is a major cause of acute gastroenteritis for which effective treatments are sorely lacking. To provide a basis for the rational design of novel antiviral agents, the main replication enzyme in Norwalk virus, the virally encoded RNA-dependent RNA polymerase (RdRP), has been expressed in an enzymatically active form, and its structure has been crystallographically determined both in the presence and absence of divalent metal cations. Although the overall fold of the enzyme is similar to that seen previously in the RdRP from rabbit hemorrhagic disease virus, the carboxyl terminus, surprisingly, is located in the active site cleft in five independent copies of the protein in three distinct crystal forms. The location of this carboxyl-terminal segment appears to interfere with the binding of double-stranded RNA in the active site cleft and may play a role in the initiation of RNA synthesis or mediate interactions with accessory replication proteins. Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft.,Ng KK, Pendas-Franco N, Rojo J, Boga JA, Machin A, Alonso JM, Parra F J Biol Chem. 2004 Apr 16;279(16):16638-45. Epub 2004 Feb 5. PMID:14764591[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|