C‐terminal dimerization of apo‐cyclic AMP receptor protein validated in solution

Although cyclic AMP receptor protein (CRP) has long served as a typical example of effector‐mediated protein allostery, mechanistic details into its regulation have been controversial due to discrepancy between the known crystal structure and NMR structure of apo‐CRP. Here, we report that the recomb...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 2017-04, Vol.591 (7), p.1064-1070
Main Authors: Sim, Dae‐Won, Choi, Jae Wan, Kim, Ji‐Hun, Ryu, Kyoung‐Seok, Kim, Myeongkyu, Yu, Hee‐Wan, Jo, Ku‐Sung, Kim, Eun‐Hee, Seo, Min‐Duk, Jeon, Young Ho, Lee, Bong‐Jin, Kim, Young Pil, Won, Hyung‐Sik
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Apoproteins - chemistry
Apoproteins - genetics
Apoproteins - metabolism
Circular Dichroism
Cyclic AMP - chemistry
Cyclic AMP - metabolism
cyclic AMP receptor protein
Cyclic AMP Receptor Protein - chemistry
Cyclic AMP Receptor Protein - genetics
Cyclic AMP Receptor Protein - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Magnetic Resonance Spectroscopy
Models, Molecular
NMR spectroscopy
protein allostery
Protein Binding
Protein Domains
Protein Multimerization
Protein Structure, Secondary
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Solutions - chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Although cyclic AMP receptor protein (CRP) has long served as a typical example of effector‐mediated protein allostery, mechanistic details into its regulation have been controversial due to discrepancy between the known crystal structure and NMR structure of apo‐CRP. Here, we report that the recombinant protein corresponding to its C‐terminal DNA‐binding domain (CDD) forms a dimer. This result, together with structural information obtained in the present NMR study, is consistent with the previous crystal structure and validates its relevance also in solution. Therefore, our findings suggest that dissociation of the CDD may be critically involved in cAMP‐induced allosteric activation of CRP.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12613