1hei: Difference between revisions

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[[Image:1hei.png|left|200px]]
==STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN==
<StructureSection load='1hei' size='340' side='right' caption='[[1hei]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hei]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HEI FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
<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=1hei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hei OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hei RCSB], [http://www.ebi.ac.uk/pdbsum/1hei PDBsum]</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/he/1hei_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 ==
Helicases are nucleotide triphosphate (NTP)-dependent enzymes responsible for unwinding duplex DNA and RNA during genomic replication. The 2.1 A resolution structure of the HCV helicase from the positive-stranded RNA hepatitis C virus reveals a molecule with distinct NTPase and RNA binding domains. The structure supports a mechanism of helicase activity involving initial recognition of the requisite 3' single-stranded region on the nucleic acid substrate by a conserved arginine-rich sequence on the RNA binding domain. Comparison of crystallographically independent molecules shows that rotation of the RNA binding domain involves conformational changes within a conserved TATPP sequence and untwisting of an extended antiparallel beta-sheet. Location of the TATPP sequence at the end of an NTPase domain beta-strand structurally homologous to the 'switch region' of many NTP-dependent enzymes offers the possibility that domain rotation is coupled to NTP hydrolysis in the helicase catalytic cycle.


{{STRUCTURE_1hei|  PDB=1hei  |  SCENE=  }}
Structure of the hepatitis C virus RNA helicase domain.,Yao N, Hesson T, Cable M, Hong Z, Kwong AD, Le HV, Weber PC Nat Struct Biol. 1997 Jun;4(6):463-7. PMID:9187654<ref>PMID:9187654</ref>


===STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_9187654}}
 
==About this Structure==
[[1hei]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HEI OCA].


==See Also==
==See Also==
*[[Helicase|Helicase]]
*[[Helicase|Helicase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:009187654</ref><ref group="xtra">PMID:015048824</ref><ref group="xtra">PMID:015479787</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Viruses]]
[[Category: Viruses]]
[[Category: Weber, P.]]
[[Category: Weber, P.]]