2pl3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 3: Line 3:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pl3]] is a 1 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=2PL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PL3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pl3]] is a 1 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=2PL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PL3 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<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=2pl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pl3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pl3 RCSB], [http://www.ebi.ac.uk/pdbsum/2pl3 PDBsum]</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=2pl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pl3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pl3 RCSB], [http://www.ebi.ac.uk/pdbsum/2pl3 PDBsum]</span></td></tr>
<table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/DDX10_HUMAN DDX10_HUMAN]] Putative ATP-dependent RNA helicase.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 30: Line 32:
</StructureSection>
</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: Busam, R D.]]
[[Category: Busam, R D]]
[[Category: Collins, R.]]
[[Category: Collins, R]]
[[Category: Dahlgren, L G.]]
[[Category: Dahlgren, L G]]
[[Category: Edwards, A.]]
[[Category: Edwards, A]]
[[Category: Flodin, S.]]
[[Category: Flodin, S]]
[[Category: Flores, A.]]
[[Category: Flores, A]]
[[Category: Graslund, S.]]
[[Category: Graslund, S]]
[[Category: Hallberg, B M.]]
[[Category: Hallberg, B M]]
[[Category: Hammarstrom, M.]]
[[Category: Hammarstrom, M]]
[[Category: Holmberg-Schiavone, L.]]
[[Category: Holmberg-Schiavone, L]]
[[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: Lehtio, L.]]
[[Category: Lehtio, L]]
[[Category: Moche, M.]]
[[Category: Moche, M]]
[[Category: Nordlund, P.]]
[[Category: Nordlund, P]]
[[Category: Nyman, T.]]
[[Category: Nyman, T]]
[[Category: Persson, C.]]
[[Category: Persson, C]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Structural genomic]]
[[Category: Sagemark, J.]]
[[Category: Sagemark, J]]
[[Category: Stenmark, P.]]
[[Category: Stenmark, P]]
[[Category: Sundstrom, M.]]
[[Category: Sundstrom, M]]
[[Category: Thorsell, A G.]]
[[Category: Thorsell, A G]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J]]
[[Category: Dead]]
[[Category: Dead]]
[[Category: Helicase]]
[[Category: Helicase]]
Line 63: Line 65:
[[Category: Rna]]
[[Category: Rna]]
[[Category: Sgc]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]

Revision as of 02:47, 25 December 2014

Human DEAD-box RNA helicase DDX10, DEAD domain in complex with ADPHuman DEAD-box RNA helicase DDX10, DEAD domain in complex with ADP

Structural highlights

2pl3 is a 1 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:DDX10 (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[DDX10_HUMAN] Putative ATP-dependent RNA helicase.

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.

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

2pl3, resolution 2.15Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA