1e5t

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANTPROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

Structural highlights 1e5t is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1qfm, 1qfs Activity: Prolyl oligopeptidase, with EC number 3.4.21.26 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis. Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.,Fulop V, Szeltner Z, Polgar L EMBO Rep. 2000 Sep;1(3):277-81. PMID:11256612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Prolyl Endopeptidase

spinqualitylabelsall models 1e5t, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image