5DTU
Crystal structure of the RNA-helicase Prp28 from Chaetomium thermophilum bound to ADP
Summary for 5DTU
| Entry DOI | 10.2210/pdb5dtu/pdb |
| Descriptor | Prp28, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | dead-box protein, atpase, rna-helicase, ddx23, hydrolase |
| Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Total number of polymer chains | 1 |
| Total formula weight | 53415.10 |
| Authors | Tauchert, M.J.,Ficner, R. (deposition date: 2015-09-18, release date: 2016-05-04, Last modification date: 2024-01-10) |
| Primary citation | Tauchert, M.J.,Ficner, R. Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum. Acta Crystallogr.,Sect.F, 72:409-416, 2016 Cited by PubMed Abstract: Prp28 (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 Å resolution and is compared with the available structures of homologues. PubMed: 27139834DOI: 10.1107/S2053230X16006038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.199 Å) |
Structure validation
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