4RR1
re-refinement of entry 1sot, Crystal Structure of the DegS stress sensor
Summary for 4RR1
| Entry DOI | 10.2210/pdb4rr1/pdb |
| Descriptor | Protease degS, PHOSPHATE ION, NICKEL (II) ION, ... (4 entities in total) |
| Functional Keywords | stress response, protein quality control, pdz, upr, htra, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 103215.36 |
| Authors | Sauer, R.T.,Grant, R.A. (deposition date: 2014-11-05, release date: 2015-03-11, Last modification date: 2015-03-18) |
| Primary citation | de Regt, A.K.,Kim, S.,Sohn, J.,Grant, R.A.,Baker, T.A.,Sauer, R.T. A Conserved Activation Cluster Is Required for Allosteric Communication in HtrA-Family Proteases. Structure, 23:517-526, 2015 Cited by PubMed Abstract: In E. coli, outer-membrane stress causes a transcriptional response through a signaling cascade initiated by DegS cleavage of a transmembrane antisigma factor. Each subunit of DegS, an HtrA-family protease, contains a protease domain and a PDZ domain. The trimeric protease domain is autoinhibited by the unliganded PDZ domains. Allosteric activation requires binding of unassembled outer-membrane proteins (OMPs) to the PDZ domains and protein substrate binding. Here, we identify a set of DegS residues that cluster together at subunit-subunit interfaces in the trimer, link the active sites and substrate binding sites, and are crucial for stabilizing the active enzyme conformation in response to OMP signaling. These residues are conserved across the HtrA-protease family, including orthologs linked to human disease, supporting a common mechanism of allosteric activation. Indeed, mutation of residues at homologous positions in the DegP quality-control protease also eliminates allosteric activation. PubMed: 25703375DOI: 10.1016/j.str.2015.01.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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