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Computer-Assisted Docking Of Flavodoxin With The Atp:Co(I)Rrinoid Adenosyltransferase (Coba) Enzyme Reveals Residues Critical For Protein-Protein Interactions But Not For Catalysis*, Nicole R. Buan, Jorge C. Escalante-Semerena
Computer-Assisted Docking Of Flavodoxin With The Atp:Co(I)Rrinoid Adenosyltransferase (Coba) Enzyme Reveals Residues Critical For Protein-Protein Interactions But Not For Catalysis*, Nicole R. Buan, Jorge C. Escalante-Semerena
Department of Biochemistry: Faculty Publications
The activity of the housekeeping ATP:co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica sv. Typhimurium is required to adenosylate de novo biosynthetic intermediates of adenosylcobalamin and to salvage incomplete and complete corrinoids from the environment of this bacterium. In vitro, reduced flavodoxin (FldA) provides an electron to generate the co(I)rrinoid substrate in the CobA active site. To understand how CobAand FldA interact, a computer model of aCobA∙FldA complex was generated. This model was used to guide the introduction of mutations into CobA using site-directed mutagenesis and the synthesis of a peptide mimic of FldA. Residues Arg-9 and Arg-165 of CobA …
Computer-Assisted Docking Of Flavodoxin With The Atp:Co(I)Rrinoid Adenosyltransferase (Coba) Enzyme Reveals Residues Critical For Protein-Protein Interactions But Not For Catalysis, Nicole R. Baun, Jorge C. Escalante-Semerena
Computer-Assisted Docking Of Flavodoxin With The Atp:Co(I)Rrinoid Adenosyltransferase (Coba) Enzyme Reveals Residues Critical For Protein-Protein Interactions But Not For Catalysis, Nicole R. Baun, Jorge C. Escalante-Semerena
Department of Biochemistry: Faculty Publications
The activity of the housekeeping ATP:co(I)rrinoid adenosyltransferase
(CobA) enzyme of Salmonella enterica sv. Typhimurium
is required to adenosylate de novo biosynthetic intermediates
of adenosylcobalamin and to salvage incomplete and complete
corrinoids from the environment of this bacterium. In vitro,
reduced flavodoxin (FldA) provides an electron to generate the
co(I)rrinoid substrate in the CobA active site. To understand how
CobAand FldA interact, a computer model of aCobA-FldA complex
was generated. This model was used to guide the introduction of
mutations into CobA using site-directed mutagenesis and the synthesis
of a peptide mimic of FldA. Residues Arg-9 and Arg-165 of
CobA …