Factors Modulating Conformational Equilibria in Large Modular Proteins: A Case Study with Cobalamin-Dependent Methionine Synthase

In the course of catalysis or signaling, large multimodular proteins often undergo conformational changes that reposition the modules with respect to one another. The mechanisms that direct the reorganization of modules in these proteins are of considerable importance, but distinguishing alternate c...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2003-07, Vol.100 (14), p.8156-8163
Hauptverfasser:	Bandarian, Vahe, Ludwig, Martha L., Matthews, Rowena G.
Format:	Artikel
Sprache:	eng
Schlagworte:	5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - chemistry 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - genetics Absorption spectra Amino Acid Substitution Biochemistry Biological Sciences Case studies Catalysis Cobalt Crystal structure Enzymes Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Homocysteine - metabolism Ligands Methionine - biosynthesis Methylation Mutation, Missense Protein Binding Protein Conformation Protein Structure, Tertiary Proteins Recombinant Fusion Proteins - chemistry S-Adenosylmethionine - metabolism Spectrophotometry, Ultraviolet Structure-Activity Relationship Substrate Specificity Temperature Tetrahydrofolates - metabolism Vitamin B 12 - analogs & derivatives Vitamin B 12 - chemistry Wavelengths
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