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Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.

Aspartate transcarbamoylase from Escherichia coli is a dodecameric enzyme consisting of two trimeric catalytic subunits and three dimeric regulatory subunits. Asp-100, from one catalytic chain, is involved in stabilizing the C1-C2 interface by means of its interaction with Arg-65 from an adjacent ca...

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Detalhes bibliográficos
Main Authors: Baker, D. P., Fetler, L., Keiser, R. T., Vachette, P., Kantrowitz, E. R.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 1995
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143059/
https://ncbi.nlm.nih.gov/pubmed/7757014
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