De novo design of allosterically switchable protein assemblies.

Autor: Pillai A; Department of Biochemistry, University of Washington, Seattle, WA, USA. apillai1@uw.edu.; Institute for Protein Design, University of Washington, Seattle, WA, USA. apillai1@uw.edu., Idris A; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA.; Department of Bioengineering, University of Washington, Seattle, WA, USA., Philomin A; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Weidle C; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Skotheim R; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Leung PJY; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA.; Program in Molecular Engineering, University of Washington, Seattle, WA, USA., Broerman A; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA.; Department of Chemical Engineering, University of Washington, Seattle, WA, USA., Demakis C; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA.; Graduate Program in Biological Physics, Structure, and Design, University of Washington, Seattle, WA, USA., Borst AJ; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Praetorius F; Department of Biochemistry, University of Washington, Seattle, WA, USA. flop@uw.edu.; Institute for Protein Design, University of Washington, Seattle, WA, USA. flop@uw.edu.; Institute of Science and Technology Austria (ISTA), Klosterneuburg, Austria. flop@uw.edu., Baker D; Department of Biochemistry, University of Washington, Seattle, WA, USA. dabaker@uw.edu.; Institute for Protein Design, University of Washington, Seattle, WA, USA. dabaker@uw.edu.

Publikováno v: Nature [Nature] 2024 Aug; Vol. 632 (8026), pp. 911-920. Date of Electronic Publication: 2024 Aug 14.

Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism.

Autor: Lee, B H, Ley, B W, Kantrowitz, E R, O'Leary, M H, Wedler, F C

Publikováno v: Journal of Biological Chemistry; June 1995, Vol. 270 Issue: 26 p15620-7, 8p

Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase.

Autor: Sakash, J B, Chan, R S, Tsuruta, H, Kantrowitz, E R

Publikováno v: Journal of Biological Chemistry; January 2000, Vol. 275 Issue: 2 p752-8, 7p

Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase.

Autor: Middleton, S A, Kantrowitz, E R

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America; August 1986, Vol. 83 Issue: 16 p5866-5870, 5p

Regulatory Behavior of Escherichia coliAspartate Transcarbamylase Altered by Site-specific Mutation of Tyr240→ Phe in the Catalytic Chain

Autor: Wedler, F C, Hsuanyu, Y C, Kantrowitz, E R, Middleton, S A

Publikováno v: Journal of Biological Chemistry; October 1989, Vol. 264 Issue: 29 p17266-17274, 9p