4QHG: Crystal Structure Of Methanocaldococcus Jannaschii Dimeric Selecase

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.
PDB ID: 4QHGDownload
MMDB ID: 121578
PDB Deposition Date: 2014/5/28
Updated in MMDB: 2014/10
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 4QHG: dimeric; determined by author and by software (PISA)
Molecular Components in 4QHG
Label Count Molecule
Proteins (2 molecules)
Uncharacterized Protein Mj1213(Gene symbol: MJ_RS06490)
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB