Ligand Binding Induces a Large Conformational Change in O -Acetylserine Sulfhydrylase from Salmonella typhimurium

By Burkhard P.   Tai C-H.   Ristroph C.M.   Cook P.F.   Jansonius J.N.  

Journal of Molecular Biology, Vol. 291, Iss. 4, 1999-08 ,pp. : 941-953

Academic Press

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Resolution of Pyridoxal 5′-Phosphate from O-Acetylserine Sulfhydrylase from Salmonella typhimurium and Reconstitution of Apoenzyme with Cofactor and Cofactor Analogues as a Probe of the Cofactor Binding Site

By Schnackerz K.D.   Cook P.F.  

Archives of Biochemistry and Biophysics, Vol. 324, Iss. 1, 1995-12 ,pp. : 71-77

Elsevier

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Identification of an Allosteric Anion-binding Site on O-Acetylserine Sulfhydrylase: Structure of the Enzyme with Chloride Bound

By Burkhard P.   Tai C-H.   Jansonius J.N.   Cook P.F.  

Journal of Molecular Biology, Vol. 303, Iss. 2, 2000-10 ,pp. : 279-286

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Purification, Characterization, and Crystallization of an N-Hydroxyarylamine O-Acetyltransferase from Salmonella typhimurium

By Sinclair J.C.   delgoda R.   Noble M.E.M.   Jarmin S.   Goh N.K.   Sim E.  

Protein Expression and Purification, Vol. 12, Iss. 3, 1998-04 ,pp. : 371-380

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The Three-dimensional Solution Structure of NaD1, a New Floral Defensin from Nicotiana alata and its Application to a Homology Model of the Crop Defense Protein alfAFP

By Lay F.T.   Schirra H.J.   Scanlon M.J.   Anderson M.A.   Craik D.J.  

Journal of Molecular Biology, Vol. 325, Iss. 1, 2003-01 ,pp. : 175-188

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