2JX5
Solution structure of the ubiquitin domain N-terminal to the S27a ribosomal subunit of Giardia lamblia
Summary for 2JX5
| Entry DOI | 10.2210/pdb2jx5/pdb |
| NMR Information | BMRB: 15547 |
| Descriptor | GlUb(S27a) (1 entity in total) |
| Functional Keywords | ubiquitin, ribosome, recombination, glub, evolution, ribosomal protein |
| Biological source | Giardia lamblia ATCC 50803 |
| Total number of polymer chains | 1 |
| Total formula weight | 7304.32 |
| Authors | Catic, A.,Sun, Z.J.,Ratner, D.M.,Misaghi, S.,Spooner, E.,Samuelson, J.,Wagner, G.,Ploegh, H.L. (deposition date: 2007-11-07, release date: 2007-12-04, Last modification date: 2024-05-29) |
| Primary citation | Catic, A.,Sun, Z.J.,Ratner, D.M.,Misaghi, S.,Spooner, E.,Samuelson, J.,Wagner, G.,Ploegh, H.L. Sequence and structure evolved separately in a ribosomal ubiquitin variant EMBO J., 26:3474-3483, 2007 Cited by PubMed Abstract: Encoded by a multigene family, ubiquitin is expressed in the form of three precursor proteins, two of which are fusions to the ribosomal subunits S27a and L40. Ubiquitin assists in ribosome biogenesis and also functions as a post-translational modifier after its release from S27a or L40. However, several species do not conserve the ribosomal ubiquitin domains. We report here the solution structure of a distant variant of ubiquitin, found at the N-terminus of S27a in Giardia lamblia, referred to as GlUb(S27a). Despite the considerable evolutionary distance that separates ubiquitin from GlUb(S27a), the structure of GlUb(S27a) is largely identical to that of ubiquitin. The variant domain remains attached to S27a and is part of the assembled holoribosome. Thus, conservation of tertiary structure suggests a role of this variant as a chaperone, while conservation of the primary structure--necessary for ubiquitin's function as a post-translational modifier--is no longer required. Based on these observations, we propose a model to explain the origin of the widespread ubiquitin superfold in eukaryotes. PubMed: 17599068DOI: 10.1038/sj.emboj.7601772 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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