Disruption of quaternary structure in Escherichia coli dihydrodipicolinate synthase (DHDPS) generates a functional monomer that is no longer inhibited by lysine-Reference-Cited by-同舟云学术

Disruption of quaternary structure in Escherichia coli dihydrodipicolinate synthase (DHDPS) generates a functional monomer that is no longer inhibited by lysine

Published:2010-11 Issue:2 Volume:503 Page:202-206
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Muscroft-Taylor Andrew C.,Catchpole Ryan J.,Dobson Renwick C.J.,Pearce F. Grant,Perugini Matthew A.,Gerrard Juliet A.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference29 articles.

1. Structural Symmetry and Protein Function

2. Assembly reflects evolution of protein complexes

3. The importance of being dimeric

4. Morpheeins – a new structural paradigm for allosteric regulation

5. Protein oligomerization: How and why

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