3llm
Crystal Structure Analysis of a RNA HelicaseCrystal Structure Analysis of a RNA Helicase
Structural highlights
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 PubMedRNA helicases of the DExD/H-box superfamily are critically involved in all RNA-related processes. No crystal structures of human DExH-box domains had been determined previously, and their structures were difficult to predict owing to the low level of homology among DExH-motif-containing proteins from diverse species. Here we present the crystal structures of the conserved domain 1 of the DEIH-motif-containing helicase DHX9 and of the DEAD-box helicase DDX20. Both contain a RecA-like core, but DHX9 differs from DEAD-box proteins in the arrangement of secondary structural elements and is more similar to viral helicases such as NS3. The N-terminus of the DHX9 core contains two long alpha-helices that reside on the surface of the core without contributing to nucleotide binding. The RNA-polymerase-II-interacting minimal transactivation domain sequence forms an extended loop structure that resides in a hydrophobic groove on the surface of the DEIH domain. DHX9 lacks base-selective contacts and forms an unspecific but important stacking interaction with the base of the bound nucleotide, and our biochemical analysis confirms that the protein can hydrolyze ATP, guanosine 5'-triphosphate, cytidine 5'-triphosphate, and uridine 5'-triphosphate. Together, these findings allow the localization of functional motifs within the three-dimensional structure of a human DEIH helicase and show how these enzymes can bind nucleotide with high affinity in the absence of a Q-motif. Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein.,Schutz P, Wahlberg E, Karlberg T, Hammarstrom M, Collins R, Flores A, Schuler H J Mol Biol. 2010 Jul 23;400(4):768-82. Epub 2010 May 25. PMID:20510246[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- Homo sapiens
- Arrowsmith, C H
- Berg, S Van Den
- Berglund, H
- Bountra, C
- Collins, R
- Flodin, S
- Flores, A
- Graslund, S
- Hammarstrom, M
- Johansson, A
- Johansson, I
- Kallas, A
- Karlberg, T
- Kotenyova, T
- Kotzsch, A
- Kraulis, P
- Markova, N
- Moche, M
- Nielsen, T K
- Nordlund, P
- Nyman, T
- Persson, C
- Roos, A K
- Structural genomic
- Schuler, H M
- Schutz, P
- Siponen, M I
- Svensson, L
- Thorsell, A G
- Tresaugues, L
- Wahlberg, E
- Weigelt, J
- Welin, M
- Wisniewska, M
- Activator
- Alpha-beta-alpha
- Atp-binding
- Dna-binding
- Helicase
- Hydrolase
- Methylation
- Nucleotide-binding
- Nucleus
- Phosphoprotein
- Rna-binding
- Sgc