3ly5: Difference between revisions

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[[Image:3ly5.png|left|200px]]
==DDX18 dead-domain==
<StructureSection load='3ly5' size='340' side='right' caption='[[3ly5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ly5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LY5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3ly5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ly5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ly5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ly5 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/ly/3ly5_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 ==
DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.


{{STRUCTURE_3ly5|  PDB=3ly5  |  SCENE=  }}
Comparative structural analysis of human DEAD-box RNA helicases.,Schutz P, Karlberg T, van den Berg S, Collins R, Lehtio L, Hogbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarstrom M, Moche M, Thorsell AG, Schuler H PLoS One. 2010 Sep 30;5(9). pii: e12791. PMID:20941364<ref>PMID:20941364</ref>


===DDX18 dead-domain===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_20941364}}
 
==About this Structure==
[[3ly5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LY5 OCA].


==See Also==
==See Also==
*[[Helicase|Helicase]]
*[[Helicase|Helicase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020941364</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith, C H]]
[[Category: Berg, S Van Den.]]
[[Category: Berg, S Van Den]]
[[Category: Berglund, H.]]
[[Category: Berglund, H]]
[[Category: Bountra, C.]]
[[Category: Bountra, C]]
[[Category: Collins, R.]]
[[Category: Collins, R]]
[[Category: Edwards, A M.]]
[[Category: Edwards, A M]]
[[Category: Flodin, S.]]
[[Category: Flodin, S]]
[[Category: Flores, A.]]
[[Category: Flores, A]]
[[Category: Graslund, S.]]
[[Category: Graslund, S]]
[[Category: Hammarstrom, M.]]
[[Category: Hammarstrom, M]]
[[Category: Johansson, A.]]
[[Category: Johansson, A]]
[[Category: Johansson, I.]]
[[Category: Johansson, I]]
[[Category: Kallas, A.]]
[[Category: Kallas, A]]
[[Category: Karlberg, T.]]
[[Category: Karlberg, T]]
[[Category: Kotenyova, T.]]
[[Category: Kotenyova, T]]
[[Category: Kotzsch, A.]]
[[Category: Kotzsch, A]]
[[Category: Kraulis, P.]]
[[Category: Kraulis, P]]
[[Category: Markova, N.]]
[[Category: Markova, N]]
[[Category: Moche, M.]]
[[Category: Moche, M]]
[[Category: Nielsen, T K.]]
[[Category: Nielsen, T K]]
[[Category: Nordlund, P.]]
[[Category: Nordlund, P]]
[[Category: Nyman, T.]]
[[Category: Nyman, T]]
[[Category: Persson, C.]]
[[Category: Persson, C]]
[[Category: Roos, A K.]]
[[Category: Roos, A K]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Structural genomic]]
[[Category: Schuler, H M.]]
[[Category: Schuler, H M]]
[[Category: Schutz, P.]]
[[Category: Schutz, P]]
[[Category: Siponen, M I.]]
[[Category: Siponen, M I]]
[[Category: Svensson, L.]]
[[Category: Svensson, L]]
[[Category: Thorsell, A G.]]
[[Category: Thorsell, A G]]
[[Category: Tresaugues, L.]]
[[Category: Tresaugues, L]]
[[Category: Wahlberg, E.]]
[[Category: Wahlberg, E]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J]]
[[Category: Welin, M.]]
[[Category: Welin, M]]
[[Category: Wisniewska, M.]]
[[Category: Wisniewska, M]]
[[Category: Alpha-beta]]
[[Category: Alpha-beta]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
Line 58: Line 75:
[[Category: Rna-binding]]
[[Category: Rna-binding]]
[[Category: Sgc]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]

Revision as of 12:51, 9 December 2014

DDX18 dead-domainDDX18 dead-domain

Structural highlights

3ly5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:DDX18 (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

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 PubMed

DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.

Comparative structural analysis of human DEAD-box RNA helicases.,Schutz P, Karlberg T, van den Berg S, Collins R, Lehtio L, Hogbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarstrom M, Moche M, Thorsell AG, Schuler H PLoS One. 2010 Sep 30;5(9). pii: e12791. PMID:20941364[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Schutz P, Karlberg T, van den Berg S, Collins R, Lehtio L, Hogbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarstrom M, Moche M, Thorsell AG, Schuler H. Comparative structural analysis of human DEAD-box RNA helicases. PLoS One. 2010 Sep 30;5(9). pii: e12791. PMID:20941364 doi:10.1371/journal.pone.0012791

3ly5, resolution 2.80Å

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OCA
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