Reversible unfolding of dimeric phosphofructokinase-2 fromEscherichia colireveals a dominant role of inter-subunit contacts for stability
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2009.05.034/fullpdf
Reference33 articles.
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3. Structures of Staphylococcus aureus d-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism;Miallau;J. Biol. Chem.,2007
4. Structure of thermus thermophilus 2-keto-3-deoxygluconate kinase: evidence for recognition of an open chain substrate;Ohshima;J. Mol. Biol.,2004
5. Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition;Cabrera;J. Mol. Biol.,2008
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