Induced structure of a helical switch as a mechanism to regulate enzymatic activity.
Herpesviruses encode a protease that is activated by homodimerization at high enzyme concentrations during lytic replication. The homodimer contains two active sites, which are distal from the dimer interface. Assignment of backbone NMR resonances and engineering of a redox switch show that two helices position a loop containing catalytic residues within each active site.
Nomura
Anson M
AM
Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143, USA.
Marnett
Alan B
AB
Shimba
Nobuhisa
N
Dötsch
Volker
V
Craik
Charles S
CS
D001665:Binding Sites; D002384:Catalysis; D019281:Dimerization; D019288:Herpesvirus 8, Human / Q000201:enzymology*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D015202:Protein Engineering; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
D012697:Serine Endopeptidases; C107889:human herpesvirus 8 protease