5JN6
The NMR Solution Structure of RPA3313
Summary for 5JN6
| Entry DOI | 10.2210/pdb5jn6/pdb |
| NMR Information | BMRB: 30070 |
| Descriptor | Uncharacterized protein (1 entity in total) |
| Functional Keywords | ribosome, protein-protein interaction, structural genomics, structural genomics consortium, sgc, unknown function |
| Biological source | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
| Total number of polymer chains | 1 |
| Total formula weight | 9887.64 |
| Authors | Catazaro, J.,Lowe, A.J.,Powers, R.,Structural Genomics Consortium (SGC) (deposition date: 2016-04-29, release date: 2016-05-11, Last modification date: 2024-05-15) |
| Primary citation | Catazaro, J.,Lowe, A.J.,Cerny, R.L.,Powers, R. The NMR solution structure and function of RPA3313: a putative ribosomal transport protein from Rhodopseudomonas palustris. Proteins, 85:93-102, 2017 Cited by PubMed Abstract: Protein function elucidation often relies heavily on amino acid sequence analysis and other bioinformatics approaches. The reliance is extended to structure homology modeling for ligand docking and protein-protein interaction mapping. However, sequence analysis of RPA3313 exposes a large, unannotated class of hypothetical proteins mostly from the Rhizobiales order. In the absence of sequence and structure information, further functional elucidation of this class of proteins has been significantly hindered. A high quality NMR structure of RPA3313 reveals that the protein forms a novel split ββαβ fold with a conserved ligand binding pocket between the first β-strand and the N-terminus of the α-helix. Conserved residue analysis and protein-protein interaction prediction analyses reveal multiple protein binding sites and conserved functional residues. Results of a mass spectrometry proteomic analysis strongly point toward interaction with the ribosome and its subunits. The combined structural and proteomic analyses suggest that RPA3313 by itself or in a larger complex may assist in the transportation of substrates to or from the ribosome for further processing. Proteins 2016; 85:93-102. © 2016 Wiley Periodicals, Inc. PubMed: 27802574DOI: 10.1002/prot.25201 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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