title: Induced structure of a helical switch as a mechanism to regulate enzymatic activity.
abstract: 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.
authors.affiliation: Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143, USA.
authors.forename: Anson M
authors.initials: AM
authors.lastname: Nomura
authors.forename: Alan B
authors.initials: AB
authors.lastname: Marnett
authors.forename: Nobuhisa
authors.initials: N
authors.lastname: Shimba
authors.forename: Volker
authors.initials: V
authors.lastname: Dötsch
authors.forename: Charles S
authors.initials: CS
authors.lastname: Craik
mesh_terms: 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
chemical_list: D012697:Serine Endopeptidases; C107889:human herpesvirus 8 protease