CUTINASE, A199C MUTANT
Accession | 1cuu |
Experiment type | X-ray |
Resolution | 1.69 Å |
Chains | A |
Released | 11 July 1996 |
Chain A ( P00590)
References
1. Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Longhi, S., Nicolas, A., Creveld, L., Egmond, M., Verrips, C.T., de Vlieg, J., Martinez, C., Cambillau, C. Proteins 26, 442-458, (1996). View articlePMID: 8990497
2. Contribution of Cutinase Ser 42 Side-Chain to the Stabilization of the Oxyanion Transition State Nicolas, A., Egmond, M., Verrips, C.T., De Vlieg, J., Longhi, S., Cambillau, C., Martinez, C. To be published ().
3. Cutinase, a Lipolytic Enzyme with a Preformed Oxyanion Hole Martinez, C., Nicolas, A., Van Tilbeurgh, H., Egloff, M.P., Cudrey, C., Verger, R., Cambillau, C. Biochemistry 33, 83, (1994).
4. Engineering Cysteine Mutants to Obtain Crystallographic Phases with a Cutinase from Fusarium Solani Pisi Martinez, C., De Geus, P., Stanssens, P., Lauwereys, M., Cambillau, C. Protein Eng. 6, 157, (1993).
5. Fusarium Solani Cutinase is a Lipolytic Enzyme with a Catalytic Serine Accessible to Solvent Martinez, C., De Geus, P., Lauwereys, M., Matthyssens, G., Cambillau, C. Nature 356, 615, (1992).