3SNP
Crystal structure analysis of iron regulatory protein 1 in complex with ferritin H IRE RNA
Replaces: 2IPYSummary for 3SNP
Entry DOI | 10.2210/pdb3snp/pdb |
Related | 2IPY 3SN2 |
Descriptor | Cytoplasmic aconitate hydratase, ferritin H IRE RNA (3 entities in total) |
Functional Keywords | rna binding, iron sulfur cluster binding, phosphorylation, lyase-rna complex, lyase/rna |
Biological source | Oryctolagus cuniculus (rabbit) |
Cellular location | Cytoplasm: Q01059 |
Total number of polymer chains | 4 |
Total formula weight | 220690.82 |
Authors | Volz, K.,Selezneva, A.I.,Walden, W.E. (deposition date: 2011-06-29, release date: 2011-07-27, Last modification date: 2023-09-13) |
Primary citation | Walden, W.E.,Selezneva, A.I.,Dupuy, J.,Volbeda, A.,Fontecilla-Camps, J.C.,Theil, E.C.,Volz, K. Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. Science, 314:1903-1908, 2006 Cited by PubMed Abstract: Iron regulatory protein 1 (IRP1) binds iron-responsive elements (IREs) in messenger RNAs (mRNAs), to repress translation or degradation, or binds an iron-sulfur cluster, to become a cytosolic aconitase enzyme. The 2.8 angstrom resolution crystal structure of the IRP1:ferritin H IRE complex shows an open protein conformation compared with that of cytosolic aconitase. The extended, L-shaped IRP1 molecule embraces the IRE stem-loop through interactions at two sites separated by approximately 30 angstroms, each involving about a dozen protein:RNA bonds. Extensive conformational changes related to binding the IRE or an iron-sulfur cluster explain the alternate functions of IRP1 as an mRNA regulator or enzyme. PubMed: 17185597DOI: 10.1126/science.1133116 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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