6XKB

Crystal structure of SR-related and CTD-associated factor 4(SCAF4-CID)with peptide S2,S5p-CTD

Summary for 6XKB

• Entry DOI: 10.2210/pdb6xkb/pdb
• Descriptor: SR-related and CTD-associated factor 4, S2,S5p-CTD peptide, UNKNOWN ATOM OR ION, ... (4 entities in total)
• Functional Keywords: scaf4-cid, structural genomics, structural genomics consortium, sgc, peptide binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 10
• Total formula weight: 92726.23

Authors

Zhou, M.Q.,Dong, A.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2020-06-26, release date: 2021-01-20, Last modification date: 2023-10-18)

Primary citation

Zhou, M.,Ehsan, F.,Gan, L.,Dong, A.,Li, Y.,Liu, K.,Min, J.
Structural basis for the recognition of the S2, S5-phosphorylated RNA polymerase II CTD by the mRNA anti-terminator protein hSCAF4.
Febs Lett., 596:249-259, 2022

PubMed Abstract: The C-terminal domain (CTD) of RNA polymerase II serves as a binding platform for numerous enzymes and transcription factors involved in nascent RNA processing and the transcription cycle. The S2, S5-phosphorylated CTD is recognized by the transcription factor SCAF4, which functions as a transcription anti-terminator by preventing early mRNA transcript cleavage and polyadenylation. Here, we measured the binding affinities of differently modified CTD peptides by hSCAF4 and solved the complex structure of the hSCAF4-CTD-interaction domain (CID) bound to a S2, S5-quadra-phosphorylated CTD peptide. Our results revealed that the S2, S5-quadra-phosphorylated CTD peptide adopts a trans conformation and is located in a positively charged binding groove of hSCAF4-CID. Although hSCAF4-CID has almost the same binding pattern to the CTD as other CID-containing proteins, it preferentially binds to the S2, S5-phosphorylated CTD. Our findings provide insight into the regulatory mechanism of hSCAF4 in transcription termination.

PubMed: 34897689
DOI: 10.1002/1873-3468.14256

Experimental method

X-RAY DIFFRACTION (1.6 Å)