5dtu
Crystal structure of the RNA-helicase Prp28 from Chaetomium thermophilum bound to ADPCrystal structure of the RNA-helicase Prp28 from Chaetomium thermophilum bound to ADP
Structural highlights
FunctionPublication Abstract from PubMedPrp28 (pre-mRNA-splicing ATP-dependent RNA helicase 28) is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner as well as for the formation of the pre-catalytic spliceosome, which in contrast is ATP-dependent. During the latter step, Prp28 is crucial for the integration of the U4/U6.U5 tri-snRNP since it displaces the U1 snRNP and allows the U6 snRNP to base-pair with the 5'-splice site. Here, the crystal structure of Prp28 from the thermophilic fungus Chaetomium thermophilum is reported at 3.2 A resolution and is compared with the available structures of homologues. Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum.,Tauchert MJ, Ficner R Acta Crystallogr F Struct Biol Commun. 2016 May 1;72(Pt 5):409-16. doi:, 10.1107/S2053230X16006038. Epub 2016 Apr 22. PMID:27139834[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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