2fge
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Crystal structure of presequence protease PreP from Arabidopsis thaliana
OverviewOverview
Presequence protease PreP is a novel protease that degrades targeting, peptides as well as other unstructured peptides in both mitochondria and, chloroplasts. The first structure of PreP from Arabidopsis thaliana, refined at 2.1 Angstroms resolution shows how the 995-residue polypeptide, forms a unique proteolytic chamber of more than 10,000 Angstroms(3) in, which the active site resides. Although there is no visible opening to the, chamber, a peptide is bound to the active site. The closed conformation, places previously unidentified residues from the C-terminal domain at the, active site, separated by almost 800 residues in sequence to active site, residues located in the N-terminal domain. Based on the structure, a novel, mechanism for proteolysis is proposed involving hinge-bending motions that, cause the protease to open and close in response to substrate binding. In, support of this model, cysteine double mutants designed to keep the, chamber covalently locked show no activity under oxidizing conditions. The, manner in which substrates are processed inside the chamber is reminiscent, of the proteasome; therefore, we refer to this protein as a peptidasome.
About this StructureAbout this Structure
2FGE is a Single protein structure of sequence from Arabidopsis thaliana with ZN, CL and MG as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis., Johnson KA, Bhushan S, Stahl A, Hallberg BM, Frohn A, Glaser E, Eneqvist T, EMBO J. 2006 May 3;25(9):1977-86. Epub 2006 Apr 6. PMID:16601675
Page seeded by OCA on Wed Nov 21 10:32:25 2007