1ZWZ
Structural comparison of Yeast snoRNP and splicesomal protein snu13p with its homologs
Summary for 1ZWZ
| Entry DOI | 10.2210/pdb1zwz/pdb |
| Descriptor | Snu13p (2 entities in total) |
| Functional Keywords | protein rna complex, rrna modification, mrna splicing, rna binding protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 27165.71 |
| Authors | Oruganti, S.,Zhang, Y.,Li, H. (deposition date: 2005-06-06, release date: 2006-05-23, Last modification date: 2024-02-14) |
| Primary citation | Oruganti, S.,Zhang, Y.,Li, H. Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with its homologs Biochem.Biophys.Res.Commun., 333:550-554, 2005 Cited by PubMed Abstract: Snu13p is a bifunctional yeast protein involved in both messenger RNA splicing as well as ribosomal RNA maturation. Snu13p initiates assembly of ribonucleoprotein particles by interacting with a conserved RNA motif called kink turn. Unlike its archaeal homolog, L7Ae, Snu13p displays differential specificity for functionally distinct kink turns. Thus, the structures of Snu13p at different functional states, including those alone and bound with RNAs, are required to understand how the protein differentially interacts with kink turns. Although the structure of the human homolog of Snu13p bound with a spliceosomal RNA is known, there has not been a report of a structure of free Snu13p. This has hindered our ability to understand the structural basis for Snu13p's substrate specificity. We report a crystal structure of free Snu13p at 1.9A and a detailed structural comparison with its homologs. We show that free Snu13p has nearly an identical conformation as that of its human homolog bound with RNA. Interestingly, both eukaryotic proteins exhibit notable structural differences in their central beta-sheets as compared to their archaeal homolog, L7Ae. The observed structural differences offer a possible explanation to the observed difference in RNA specificity between Snu13p and L7Ae. PubMed: 15963469DOI: 10.1016/j.bbrc.2005.05.141 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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