3fe2: Difference between revisions
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[[ | ==Human DEAD-BOX RNA helicase DDX5 (P68), conserved domain I in complex with ADP== | ||
<StructureSection load='3fe2' size='340' side='right' caption='[[3fe2]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fe2]] 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=3FE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FE2 FirstGlance]. <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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX5 ([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=3fe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fe2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fe2 RCSB], [http://www.ebi.ac.uk/pdbsum/3fe2 PDBsum]</span></td></tr> | |||
</table> | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__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: Dahlgren, L G | [[Category: Dahlgren, L G]] | ||
[[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: Karlberg, T | [[Category: Karlberg, T]] | ||
[[Category: Kotenyova, T | [[Category: Kotenyova, T]] | ||
[[Category: Lehtio, L | [[Category: Lehtio, L]] | ||
[[Category: Moche, M | [[Category: Moche, M]] | ||
[[Category: Nilsson, M E | [[Category: Nilsson, M E]] | ||
[[Category: Nordlund, P | [[Category: Nordlund, P]] | ||
[[Category: Nyman, T | [[Category: Nyman, T]] | ||
[[Category: Persson, C | [[Category: Persson, C]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Sagemark, J | [[Category: Sagemark, J]] | ||
[[Category: Schuler, H | [[Category: Schuler, H]] | ||
[[Category: Siponen, M I | [[Category: Siponen, M I]] | ||
[[Category: Thorsell, A G | [[Category: Thorsell, A G]] | ||
[[Category: Tresaugues, L | [[Category: Tresaugues, L]] | ||
[[Category: Weigelt, J | [[Category: Weigelt, J]] | ||
[[Category: Welin, M | [[Category: Welin, M]] | ||
[[Category: Wikstrom, M | [[Category: Wikstrom, M]] | ||
[[Category: Wisniewska, M | [[Category: Wisniewska, M]] | ||
[[Category: Adp]] | [[Category: Adp]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
Line 59: | Line 66: | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
[[Category: Spliceosome]] | [[Category: Spliceosome]] | ||
Revision as of 11:35, 26 November 2014
Human DEAD-BOX RNA helicase DDX5 (P68), conserved domain I in complex with ADPHuman DEAD-BOX RNA helicase DDX5 (P68), conserved domain I in complex with ADP
Structural highlights
Publication Abstract from PubMedDEAD-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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Homo sapiens
- Arrowsmith, C H
- Berg, S Van Den
- Berglund, H
- Bountra, C
- Collins, R
- Dahlgren, L G
- Edwards, A M
- Flodin, S
- Flores, A
- Graslund, S
- Hammarstrom, M
- Johansson, A
- Johansson, I
- Karlberg, T
- Kotenyova, T
- Lehtio, L
- Moche, M
- Nilsson, M E
- Nordlund, P
- Nyman, T
- Persson, C
- Structural genomic
- Sagemark, J
- Schuler, H
- Siponen, M I
- Thorsell, A G
- Tresaugues, L
- Weigelt, J
- Welin, M
- Wikstrom, M
- Wisniewska, M
- Adp
- Atp-binding
- Dead
- Helicase
- Hydrolase
- Methylation
- Mrna processing
- Mrna splicing
- Nucleotide-binding
- Nucleus
- Phosphoprotein
- Rna helicase
- Rna-binding
- Sgc
- Spliceosome