1OU8
structure of an AAA+ protease delivery protein in complex with a peptide degradation tag
Summary for 1OU8
| Entry DOI | 10.2210/pdb1ou8/pdb |
| Related | 1OU9 1OUL |
| Descriptor | Stringent starvation protein B homolog, synthetic ssrA peptide, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | peptide-binding pocket, protein-peptide complex, homodimer, transport protein |
| Biological source | Haemophilus influenzae More |
| Total number of polymer chains | 4 |
| Total formula weight | 27739.41 |
| Authors | Levchenko, I.,Grant, R.A.,Wah, D.A.,Sauer, R.T.,Baker, T.A. (deposition date: 2003-03-24, release date: 2003-09-23, Last modification date: 2023-08-16) |
| Primary citation | Levchenko, I.,Grant, R.A.,Wah, D.A.,Sauer, R.T.,Baker, T.A. Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag Mol.Cell, 12:365-372, 2003 Cited by PubMed Abstract: Substrate selection by AAA+ ATPases that function to unfold proteins or alter protein conformation is often regulated by delivery or adaptor proteins. SspB is a protein dimer that binds to the ssrA degradation tag and delivers proteins bearing this tag to ClpXP, an AAA+ protease, for degradation. Here, we describe the structure of the peptide binding domain of H. influenzae SspB in complex with an ssrA peptide at 1.6 A resolution. The ssrA peptides are bound in well-defined clefts located at the extreme ends of the SspB homodimer. SspB contacts residues within the N-terminal and central regions of the 11 residue ssrA tag but leaves the C-terminal residues exposed and positioned to dock with ClpX. This structure, taken together with biochemical analysis of SspB, suggests mechanisms by which proteins like SspB escort substrates to AAA+ ATPases and enhance the specificity and affinity of target recognition. PubMed: 14536076DOI: 10.1016/j.molcel.2003.08.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
