9ZJM

Crystal structure of P. furiosus SRP54 NG domain T116del

Summary for 9ZJM

• Entry DOI: 10.2210/pdb9zjm/pdb
• Descriptor: Signal recognition particle 54 kDa protein (2 entities in total)
• Functional Keywords: gtpase, signal recognition particle, rna binding protein
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 34730.28

Authors

Yang, M.,Bruner, S.D. (deposition date: 2025-12-04, release date: 2026-10-28, Last modification date: 2026-11-04)

Primary citation

Yang, M.,Brim, A.D.,Long, L.F.,Wu, G.C.,Schlichting, G.M.,Denard, C.A.,Bruner, S.D.
Structure and Function of Archaeal SRP54 Protein Mutants Associated with Human Severe Congenital Neutropenia.
Acs Omega, 11:63170-63178, 2026

PubMed Abstract: SRP54, a key component of the signal recognition particle, is a highly conserved enzyme both structurally and functionally. The protein plays a vital role in cellular protein translocation by interacting with the translating ribosome and a membrane receptor, thereby aiding protein folding and trafficking. Recent studies have shown that mutations in the gene cause severe neutropenia and are associated with an increased risk of pediatric leukemias. Here, we present high-resolution structures of clinically relevant SRP54 mutant proteins from the archaea . This work complements existing structural and functional data on SRP54 and offers a high-resolution structural basis for clinically relevant congenital mutations. The structures of three mutants are presented along with the model wild type. Overall, the results provide a detailed understanding of how mutations affect SRP54 structure. Additionally, comparing our findings with available structures from higher eukaryotes offers new insights into the mechanisms of dysfunction.

PubMed: 42923585
DOI: 10.1021/acsomega.6c06315

Experimental method

X-RAY DIFFRACTION (1.44 Å)