5F5S
Crystal structure of the Prp38-MFAP1 complex of Homo sapiens
Summary for 5F5S
| Entry DOI | 10.2210/pdb5f5s/pdb |
| Descriptor | Pre-mRNA-splicing factor 38A, Microfibrillar-associated protein 1 (3 entities in total) |
| Functional Keywords | b-specific protein, pre-mrna splicing, sah, splicing |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Nucleus : Q8NAV1 P55081 |
| Total number of polymer chains | 2 |
| Total formula weight | 31113.70 |
| Authors | Ulrich, A.K.C.,Wahl, M.C. (deposition date: 2015-12-04, release date: 2016-10-12, Last modification date: 2024-01-10) |
| Primary citation | Ulrich, A.K.C.,Seeger, M.,Schutze, T.,Bartlick, N.,Wahl, M.C. Scaffolding in the Spliceosome via Single alpha Helices. Structure, 24:1972-1983, 2016 Cited by PubMed Abstract: The spliceosomal B complex-specific protein Prp38 forms a complex with the intrinsically unstructured proteins MFAP1 and Snu23. Our binding and crystal structure analyses show that MFAP1 and Snu23 contact Prp38 via ER/K motif-stabilized single α helices, which have previously been recognized only as rigid connectors or force springs between protein domains. A variant of the Prp38-binding single α helix of MFAP1, in which ER/K motifs not involved in Prp38 binding were mutated, was less α-helical in isolation and showed a reduced Prp38 affinity, with opposing tendencies in interaction enthalpy and entropy. Our results indicate that the strengths of single α helix-based interactions can be tuned by the degree of helix stabilization in the unbound state. MFAP1, Snu23, and several other spliceosomal proteins contain multiple regions that likely form single α helices via which they might tether several binding partners and act as intermittent scaffolds that facilitate remodeling steps during assembly of an active spliceosome. PubMed: 27773687DOI: 10.1016/j.str.2016.09.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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