Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4FAX

Structure of Oceanobacillus iheyensis group II intron in a ligand-free state in the presence of Na+ and Mg2+

Summary for 4FAX
Entry DOI10.2210/pdb4fax/pdb
Related4E8K 4E8M 4E8N 4E8P 4E8Q 4E8R 4E8T 4E8V 4FAQ 4FAR 4FAU 4FAW 4FB0
DescriptorGroup IIC intron, MAGNESIUM ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsribozyme, self-splicing, retrotransposition, spliceosome, rna
Biological sourceOceanobacillus iheyensis
Total number of polymer chains1
Total formula weight129401.03
Authors
Marcia, M.,Pyle, A.M. (deposition date: 2012-05-22, release date: 2012-11-14, Last modification date: 2023-09-13)
Primary citationMarcia, M.,Pyle, A.M.
Visualizing Group II Intron Catalysis through the Stages of Splicing.
Cell(Cambridge,Mass.), 151:497-507, 2012
Cited by
PubMed Abstract: Group II introns are self-splicing ribozymes that share a reaction mechanism and a common ancestor with the eukaryotic spliceosome, thereby providing a model system for understanding the chemistry of pre-mRNA splicing. Here we report 14 crystal structures of a group II intron at different stages of catalysis. We provide a detailed mechanism for the first step of splicing, we describe a reversible conformational change between the first and the second steps of splicing, and we present the ligand-free intron structure after splicing in an active state that corresponds to the retrotransposable form of the intron. During each reaction, the reactants are aligned and activated by a heteronuclear four-metal-ion center that contains a metal cluster and obligate monovalent cations, and they adopt a structural arrangement similar to that of protein endonucleases. Based on our data, we propose a model for the splicing cycle and show that it is applicable to the eukaryotic spliceosome.
PubMed: 23101623
DOI: 10.1016/j.cell.2012.09.033
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

227111

数据于2024-11-06公开中

PDB statisticsPDBj update infoContact PDBjnumon