3VI6
Crystal Structure of human ribosomal protein L30e
Summary for 3VI6
| Entry DOI | 10.2210/pdb3vi6/pdb |
| Descriptor | 60S ribosomal protein L30, FORMIC ACID (3 entities in total) |
| Functional Keywords | three-layer alpha/beta/alpa, ribosomal protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 13962.29 |
| Authors | Kawaguchi, A.,Ose, T.,Yao, M.,Tanaka, I. (deposition date: 2011-09-21, release date: 2011-12-21, Last modification date: 2023-11-08) |
| Primary citation | Kawaguchi, A.,Ose, T.,Yao, M.,Tanaka, I. Crystallization and preliminary X-ray structure analysis of human ribosomal protein L30e Acta Crystallogr.,Sect.F, 67:1516-1518, 2011 Cited by PubMed Abstract: Many functions have been reported for the eukaryotic ribosomal protein L30e. L30e makes several inter-subunit and intra-subunit interactions with protein or RNA components of the 80S ribosome. Yeast L30e has been shown to bind to its own transcript to autoregulate expression at both the transcriptional and the translational levels. Furthermore, it has been reported that mammalian L30e is a component of the selenocysteine-incorporation machinery by binding to the selenocysteine-insertion sequence on mRNA. As high-resolution crystal structures of mammalian L30e are not available, the purification, crystallization and X-ray structure analysis of human L30e are presented here. PubMed: 22139155DOI: 10.1107/S1744309111045131 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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