4QHF

Crystal structure of Methanocaldococcus jannaschii monomeric selecase

Summary for 4QHF

• Entry DOI: 10.2210/pdb4qhf/pdb
• Related: 4JIU 4JIX 4QHG 4QHH 4QHI 4QHJ
• Descriptor: Uncharacterized protein MJ1213, NICKEL (II) ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: minigluzincin, proteolytic enzyme, hydrolase
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 1
• Total formula weight: 13254.33

Authors

Lopez-pelegrin, M.,Cerda-costa, N.,Cintas-pedrola, A.,Herranz-trillo, F.,Bernado, P.,Peinado, J.R.,Arolas, J.L.,Gomis-ruth, F.X. (deposition date: 2014-05-28, release date: 2014-07-16, Last modification date: 2024-04-03)

Primary citation

Lopez-Pelegrin, M.,Cerda-Costa, N.,Cintas-Pedrola, A.,Herranz-Trillo, F.,Bernado, P.,Peinado, J.R.,Arolas, J.L.,Gomis-Ruth, F.X.
Multiple stable conformations account for reversible concentration-dependent oligomerization and autoinhibition of a metamorphic metallopeptidase
Angew.Chem.Int.Ed.Engl., 53:10624-10630, 2014

PubMed Abstract: Molecular plasticity controls enzymatic activity: the native fold of a protein in a given environment is normally unique and at a global free-energy minimum. Some proteins, however, spontaneously undergo substantial fold switching to reversibly transit between defined conformers, the "metamorphic" proteins. Here, we present a minimal metamorphic, selective, and specific caseinolytic metallopeptidase, selecase, which reversibly transits between several different states of defined three-dimensional structure, which are associated with loss of enzymatic activity due to autoinhibition. The latter is triggered by sequestering the competent conformation in incompetent but structured dimers, tetramers, and octamers. This system, which is compatible with a discrete multifunnel energy landscape, affords a switch that provides a reversible mechanism of control of catalytic activity unique in nature.

PubMed: 25159620
DOI: 10.1002/anie.201405727

Experimental method

X-RAY DIFFRACTION (2.1 Å)