1OX9
Crystal structure of SspB-ssrA complex
Summary for 1OX9
| Entry DOI | 10.2210/pdb1ox9/pdb |
| Related | 1OX8 |
| Descriptor | Stringent starvation protein B, ssrA (2 entities in total) |
| Functional Keywords | sspb-ssra, hydrolase activator |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 16 |
| Total formula weight | 103083.98 |
| Authors | Song, H.K.,Eck, M.J. (deposition date: 2003-04-01, release date: 2003-08-26, Last modification date: 2024-02-14) |
| Primary citation | Song, H.K.,Eck, M.J. Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine Mol.Cell, 12:75-86, 2003 Cited by PubMed Abstract: In prokaryotes, incomplete or misfolded polypeptides emanating from a stalled ribosome are marked for degradation by the addition of an 11 residue peptide (AANDENYALAA) to their C terminus. Substrates containing this conserved degradation signal, the SsrA tag, are targeted to specific proteases including ClpXP and ClpAP. SspB was originally characterized as a stringent starvation protein and has been found to bind specifically to SsrA-tagged proteins and to enhance recognition of these proteins by the ClpXP degradation machine. Here, we report the crystal structures of SspB alone and in complex with an SsrA peptide. Unexpectedly, SspB exhibits a fold found in Sm-family RNA binding proteins. The dimeric SspB structures explain the key determinants for recognition of the SsrA tag and define a hydrophobic channel that may bind unfolded substrates. PubMed: 12887894DOI: 10.1016/S1097-2765(03)00271-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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