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TitleA Conserved Activation Cluster Is Required for Allosteric Communication in HtrA-Family Proteases.
Journal, issue, pagesStructure, Vol. 23, Page 517-526, Year 2015
Publish dateNov 5, 2014 (structure data deposition date)
Authorsde Regt, A.K. / Kim, S. / Sohn, J. / Grant, R.A. / Baker, T.A. / Sauer, R.T.
External linksStructure / PubMed:25703375
MethodsX-ray diffraction
Resolution2.204 - 3.054 Å
Structure data

PDB-4rqy:
RE-REFINED STRUCTURE OF 1TE0 - STRUCTURAL ANALYSIS of DEGS, A STRESS SENSOR OF THE BACTERIAL PERIPLASM
Method: X-RAY DIFFRACTION / Resolution: 2.204 Å

PDB-4rqz:
re-refinement of 1soz, Crystal Structure of DegS protease in complex with an activating peptide
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-4rr0:
re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE
Method: X-RAY DIFFRACTION / Resolution: 3.054 Å

PDB-4rr1:
re-refinement of entry 1sot, Crystal Structure of the DegS stress sensor
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-NI:
NICKEL (II) ION

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / TWO DOMAINS / SERINE PROTEASE / PDZ / ALPHA-BETA PROTEIN / stress response / htra / Hydrolase/peptide / PROTEIN QUALITY CONTROL / UPR / Hydrolase-peptide complex

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